TITLE: Gene Expression in Horticultural Crops
PUBLICATION DATE:December, 1992
ENTRY DATE: February, 1994
EXPIRATION DATE: None
UPDATE: As needed
CONTACT: Biotechnology Information Center(biotech@nalusda.gov)
National Agricultural Library
DOCUMENT TYPE: Text
DOCUMENT SIZE: 390k, approx. 217 pp.
ISSN: 1052-5378
United States Department of Agriculture
National Agricultural Library
10301 Baltimore Blvd.
Beltsville, Maryland 20705-2351
Gene Expression in Horticultural Crops
January 1991 - October 1992
QB 93-08
Updates QB 91-109
215 citations from AGRICOLA
Robert Warmbrodt and Janet Saunders
Biotechnology Information Center
December 1992
National Agricultural Library Cataloging Record:
Warmbrodt, Robert D.
(Quick bibliography series ; 93-08)
1. Gene expression--Bibliography. 2. Horticultural crops--
Bibliography. I. Saunders, Janet. II. Title.
aZ5071.N AGRICOLA
Search Strategy
Set Items Description
S1 6582 (GENE OR GENES OR GENETIC?)(W)EXPRESS?
S2 6413 S1/TI,DE
S3 115652 HORTICULTUR? OR VEGETABLE? OR FRUIT OR
FRUITS OR NUT OR NUTS OR HERB OR HERBS
S4 6610 ASPARAGUS? OR CELERY? OR ENDIVE? OR
LETTUCE? OR PARSLEY? OR RHUBARB? OR
SPINACH?
S5 8802 BRASSICA? OR BROCCOLI? OR
BRUSSELS()SPROUT? OR CABBAGE? OR KALE? OR
KOHLRABI?
S6 8514 CANTALOUPE? OR CUCUMBER? OR CUCUMIS? OR
CUCURBIT? OR GOURD? OR MELON? OR
MUSKMELON? OR PUMPKIN? OR SQUASH? OR
WATERMELON?
S7 50458 BEAN OR BEANS OR BEET OR BEETS OR CARROT?
OR CASSAVA? OR EGGPLANT? OR GARLIC? OR
LEEK? OR OKRA? OR ONION? OR PEA OR PEAS OR
PEPPER OR PEPPERS OR POTATO?
S8 19720 RADISH? OR SHALLOT? OR SUGARBEET? OR
SUGAR()BEET? OR SWEETCORN? OR SWEET()CORN?
OR TOMATO? OR TURNIP? OR YAM OR YAMS
S9 10776 AVOCADO? OR BANANA? OR COCONUT? OR DATES
OR FIG OR FIGS OR GUAVA? OR MANGO? OR
OLIVE OR OLIVES OR PAPAYA? OR
PASSION()FRUIT? OR PINEAPPLE? OR
POMEGRANATE? OR SOURSOP? OR PERSIMMON?
S10 12061 CITRUS? OR KUMQUAT? OR LEMON? OR LIME OR
LIMES OR ORANGE?
S11 22838 APPLE? OR APRICOT? OR CHERR? OR MULBERR?
OR NECTARINE? OR PEACH? OR PEAR OR PEARS
OR PLUM OR PLUMS OR PRUNE?
S12 17093 BERR? OR BLACKBERR? OR BLUEBERR? OR
BOYSENBERR? OR CRANBERR? OR CURRANT? OR
ELDERBERR? OR GOOSEBERR? OR GRAPE? OR
KIWI? OR RASPBERR? OR STRAWBERR?
S13 5297 ALMOND? OR CHESTNUT? OR WALNUT? OR CASHEW?
OR FILBERT? OR MACADAMIA()NUT? OR PECAN?
OR HAZELNUT? OR HAZEL()NUT? OR PISTACHIO?
S14 1609 BASIL OR DILL OR GINGER OR MUSTARD OR
OREGANO OR THYME
S15 215177 S3 OR S4 OR S5 OR S6 OR S7 OR S8 OR S9 OR
S10 OR S11 OR S12 OR S13 OR S14
S16 891 S15 AND S2
S17 332 S16 AND PY=1991:1992
Gene Expression of Horticultural Crops
1 NAL Call. No.: 442.8 J8224
1-Aminocyclopropane-1-carboxylate synthase in tomato is
encoded by a multigene family whose transcription is induced
during fruit and floral senescence. Rottmann, W.H.; Peter,
G.F.; Oeller, P.W.; Keller, J.A.; Shen, N.F.; Nagy, B.P.;
Taylor, L.P.; Campbell, A.D.; Theologis, A.
London : Academic Press; 1991 Dec20.
Journal of molecular biology v. 222 (4): p. 937-961; 1991
Dec20. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Flowers; Fruits;
Ripening; Senescence; Ethylene; Biosynthesis; Enzyme activity;
Acc; Messenger RNA; Genetic regulation; Transcription; Gene
expression; Multigene families; Amino acid sequences;
Nucleotide sequences; Comparisons; Restriction mapping
Abstract: The key regulatory enzyme in the biosynthetic
pathway of the plant hormone ethylene is 1-
aminocyclopropane-1-carboxylic acid (ACC) synthase (EC
4.1.1.14). It catalyzes the conversion of S-adenosylmethionine
to ACC, the precursor of ethylene. We isolated complementary
DNA sequences, ptACC2 and ptACC4, for two distinct and
differentially regulated ACC synthase mRNAs expressed in ripe
tomato fruit. The authenticity of the, clones has been
confirmed by expression experiments in E. coli. The predicted
size of the encoded polypeptides (54,660 and 53,519 Da) is
similar to that of the primary in vitro translation products
and to the proteins found in vivo. The sequence of the gene
encoding one mRNA, LE-ACC2 has been determined and its
transcription initiation site defined. Four additional genes,
LE-ACC1A, LE-ACC1B, LE-ACC3 and LE-ACC4, have also been
identified and the sequence of their coding regions
determined. The LE-ACC1A and LE-ACC1B genes are adjacent to
each other and are convergently transcribed. Their encoded
polypeptides are 96% identical; the identity of the other
polypeptides to each other varies between 50% and 70%. The
proteins predicted to be encoded by the ACC synthase genes so
far cloned from tomato and zucchini contain 11 of the 12
conserved amino acid residues found in various
aminotransferases involved in the binding of the substrate and
the cofactor pyridoxal-5'-phosphate. The data indicate that
ACC synthase is encoded by a divergent multigene family, in
tomato that encodes proteins related to aminotransferases.
2 NAL Call. No.: QK725.P532
Abscisic acid mediates wound induction but not developmental-
specific expression of the proteinase inhibitor II gene
family.
Pena-Cortes, H.; Willmitzer, L.; Sanchez-Serrano, J.J.
Rockville, Md. : American Society of Plant Physiologists; 1991
Sep. The Plant cell v. 3 (9): p. 963-972; 1991 Sep. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Solanum tuberosum;
Solanum phureja; Multigene families; Proteinase inhibitors;
Gene expression; Genetic regulation; Abscisic acid; Abiotic
injuries; Messenger RNA; Flowers; Tubers; Leaves; Flowering
Abstract: The expression of the potato and tomato proteinase
inhibitor II (pin2) gene family is subject to both
developmental and environmental control, being constitutively
expressed in potato tubers while only being present in the
foliage of the potato or tomato plants after mechanical
damage. There is evidence that the phytohormone abscisic acid
(ABA) is involved in this wound induction of pin2 gene
expression. This paper describes experiments that demonstrate
that ABA is able to induce the expression of the pin2 gene
family, both locally and systemically, at physiological
concentrations. The significance of the ABA involvement in the
pin2 induction upon wounding has been further strengthened by
analyzing the expression of a pin2 promoter-beta-glucuronidase
gene fusion in transgenic ABA-deficient mutant potato plants.
We have analyzed the developmental regulation of pin2 gene
expression in wild-type and ABA-deficient potato and tomato
plants. The pin2 mRNA level is identical in mutant and wild-
type parental Solanum phureja tubers. In addition, evidence is
presented for pin2 also being constitutively expressed at
certain stages in the development of both tomato and potato
flowers. Again, the ABA deficiency appears to have little
influence in this tissue-specific expression in the mutants.
These results suggest the action of separate pathways for the
developmental and environmental regulation of pin2 gene
expression.
3 NAL Call. No.: QK710.P62
Accumulation of wound-inducible ACC synthase transcript in
tomato fruit is inhibited by salicylic acid and polyamines.
Li, N.; Parsons, B.L.; Liu, D.; Mattoo, A.K.
Dordrecht : Kluwer Academic Publishers; 1992 Feb.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(3): p. 477-487; 1992 Feb. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Messenger RNA; Ligases;
Acc; Fruits; Gene expression; Genetic regulation; Abiotic
injuries; Inhibition; Salicylic acid; Putrescine; Spermine;
Spermidine; Enzyme activity
Abstract: Regulation of wound-inducible 1-
aminocyclopropane-1-carboxylic acid (ACC) synthase expression
was studied in tomato fruit (Lycopersicon esculentum cv. Pik-
Red). A 70 base oligonucleotide probe homologous to published
ACC synthase cDNA sequences was successfully used to identify
and analyze regulation of a wound-inducible transcript. The
1.8 kb ACC synthase transcript increased upon wounding the
fruit as well as during fruit ripening. Salicylic acid, an
inhibitor of wound-responsive genes in tomato, inhibited the
wound-induced accumulation of the ACC synthase transcript.
Further, polyamines (putrescine, spermidine and spermine) that
have anti-senescence properties and have been shown to inhibit
the development of ACC synthase activity, inhibited the
accumulation of the wound-inducible ACC synthase transcript.
The inhibition by spermine was greater than that caused by
putrescine or spermidine. The transcript level of a wound-
repressible glycine-rich protein gene and that of the
constitutively expressed rRNA were not affected as markedly by
either salicylic acid or polyamines. These data suggest that
salicylic acid and polyamines may specifically regulate
ethylene biosynthesis at the level of ACC synthase transcript
accumulation.
4 NAL Call. No.: QK725.P532
Acquired resistance in Arabidopsis.
Uknes, S.; Mauch-Mani, B.; Moyer, M.; Potter, S.; Williams,
S.; Dincher, S.; Chandler, D.; Slusarenko, A.; Ward, E.;
Ryals, J.
Rockville, Md. : American Society of Plant Physiologists; 1992
Jun. The Plant cell v. 4 (6): p. 645-656; 1992 Jun. Includes
references.
Language: English
Descriptors: Arabidopsis thaliana; Peronospora parasitica;
Pseudomonas syringae pv. tomato; Multigene families;
Structural genes; Pathogenesis-related proteins; Nucleotide
sequences; Amino acid sequences; Gene expression; Induced
resistance; Nicotinic acid; Derivatives; Mildews; Dna
Abstract: Acquired resistance is an important component of
the complex disease resistance mechanism in plants, which can
result from either pathogen infection or treatment with
synthetic, resistance-inducing compounds. In this study,
Arabidopsis, a tractable genetic system, is shown to develop
resistance to a bacterial and a fungal pathogen following 2,6-
dichloroisonicotinic acid (INA) treatment. Three proteins that
accumulated to high levels in the apoplast in response to INA
treatment were purified and characterized. Expression of the
genes corresponding to these proteins was induced by INA,
pathogen infection, and salicylic acid, the latter being a
putative endogenous signal for acquired resistance.
Arabidopsis should serve as a genetic model for studies of
this type of immune response in plants.
5 NAL Call. No.: QK725.P532
Activity of an S locus gene promoter in pistils and anthers of
transgenic brassica.
Sato, T.; Thorsness, M.K.; Kandasamy, M.K.; Nishio, T.; Hirai,
M.; Nasrallah, J.B.; Nasrallah, M.E.
Rockville, Md. : American Society of Plant Physiologists; 1991
Sep. The Plant cell v. 3 (9): p. 867-876; 1991 Sep. Includes
references.
Language: English
Descriptors: Brassica napus var. oleifera; Brassica oleracea
var. viridis; Brassica oleracea; Promoters; Loci;
Glycoproteins; Self incompatibility; Chimeras; Beta-
glucuronidase; Reporter genes; Genetic transformation;
Transgenics; Messenger RNA; Gene expression; Histoenzymology;
Anthers; Gynoecium; Pollen; Styles
Abstract: The pollen-stigma interaction of self-
incompatibility in crucifers is correlated with glycoproteins
localized in the cell wall of the stigmatic papillae that are
encoded by the S locus glycoprotein (SLG) gene. When fused to
the beta-glucuronidase (GUS) reporter gene, the 5' upstream
regulatory region of SLG directed high level expression in the
papillae of transgenic Brassica plants. Histochemical and
fluorometric assays revealed that, in addition to its primary
site of expression in the stigmatic papillae, the SLG-GUS
fusion was also expressed in the transmitting tissue of
stigma, style, and ovary, and in anthers. This conclusion was
verified by the detection of transgene-encoded GUS transcripts
and endogenous SLG-homologous transcripts by RNA gel blot
analysis. Significantly, in anthers, the SLG promoter was
active not only sporophytically in the nurse cells of the
tapetum, but also in the haploid microspores. Because self-
incompatibility systems exhibiting sporophytic control of
pollen phenotype are thought to have evolved from systems with
gametophytic control, we suggest that sporophytic control was
acquired without loss of gametophytic function.
6 NAL Call. No.: QH426.C8
The ADP/ATP translocator from potato has a long amino-terminal
extension. Emmermann, M.; Braun, H.P.; Schmitz, U.K.
Berlin, W. Ger. : Springer International; 1991.
Current genetics v. 20 (5): p. 405-410; 1991. Includes
references.
Language: English
Descriptors: Solanum tuberosum; Genes; Plant proteins;
Mitochondria; Plasma membranes; Atp; Adp; Active transport;
Nucleotide sequences; Amino acid sequences; Gene expression
Abstract: The ADP/ATP translocator is an abundant protein of
the mitochondrial inner membrane, which in fungi and mammals
is synthesized without a presequence. Here we report that the
translocator from potato has an amino-terminal extension which
may function in mitochondrial targeting. Several cDNA clones
encoding the nucleotide sequence of the ADP/ATP translocator
have been isolated from potato leaf and tuber cDNA libraries
constructed in lambda phages. Only one class of cDNA clones
was found but possibly different translocator genes are
expressed in other tissues. High levels of transcripts for the
translocator are found in all tissues analysed. Sequence
determination of the complete insert of one of the clones
reveals a long open reading frame of 1158 bp encoding a
protein of 386 amino acids corresponding to a calculated
molecular weight of 42 kDa. In contrast, the ADP/ATP
translocator proteins from fungi and mammals are significantly
smaller. Comparison of the Neurospora translocator with the
potato protein shows about 75% sequence homology, being
confined to the region after amino acid 85 of the potato
polypeptide. Antibodies directed against the fungal
translocator recognize a protein of 30 kDa in the inner
membrane of potato mitochondria, suggesting that the mature
protein has a similar size as the translocators from fungi and
mammals. Thus, the additional segment of the potato ADP/ATP
translocator forms an amino-terminal extension which may be
involved in the import of the protein into plant mitochondria.
7 NAL Call. No.: QK725.P54
Agrobacterium-mediated transformation of Solanum tuberosum L.
cv. 'Russet Burbank'.
Newell, C.A.; Rozman, R.; Hinchee, M.A.; Lawson, E.C.; Haley,
L.; Sanders, P.; Kaniewski, W.; Tumer, N.E.; Horsch, R.B.;
Fraley, R.T.
Berlin, W. Ger. : Springer International; 1991.
Plant cell reports v. 10 (1): p. 30-34; 1991. Includes
references.
Language: English
Descriptors: Solanum tuberosum; Agrobacterium tumefaciens;
Genetic transformation; Transgenics; Coat proteins; Gene
expression; Vectors; Potato x potexvirus; Potato y potyvirus;
Genetic resistance; Regenerative ability
Abstract: Stem sections from shoot cultures maintained in
vitro were used to produce transgenic plants of the potato,
Solanum tuberosum L. cv. 'Russet Burbank'. Stem internode
pieces inoculated with Agrobacterium tumefaciens containing
coat protein genes from potato virus X and potato virus Y,
produced shoots with a frequency of 60% in the absence of
selection and 10% on medium containing 100 mg/l kanamycin
monosulfate. Regenerated shoots were assayed for kanamycin
resistance by placing stem segments on callus induction medium
containing an increased level of kanamycin. Of a total 255
regenerated shoots, 47 (18%) were kanamycin resistant. Of the
kanamycin resistant shoots, 25 (53%) expressed the PVX or PVY
coat protein genes as assayed by enzyme-linked immunosorbent
assay or Western immunoblot analysis.
8 NAL Call. No.: QK710.P62
An alternative approach for gene transfer in trees using wild-
type Agrobacterium strains.
Brasileiro, A.C.M.; Leple, J.C.; Muzzin, J.; Ounnoughi, D.;
Michel, M.F.; Jouanin, L.
Dordrecht : Kluwer Academic Publishers; 1991 Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 441-452; 1991 Sep. Includes references.
Language: English
Descriptors: Populus tremula; Populus alba; Prunus avium;
Juglans nigra; Juglans regia; Agrobacterium tumefaciens;
Agrobacterium rhizogenes; Genetic transformation; Gene
transfer; Transgenics; Hybrids; Tumors; Shoots;
Differentiation; Micropropagation; Gene expression; Reporter
genes; Beta-glucuronidase; Phosphotransferases; In vitro
selection; Tree breeding; Crown gall
Abstract: Micropropagated shoots of three forest tree
species, poplar (Populus tremula X P. alba), wild cherry
(Prunus avium L.) and walnut (Juglans nigra X J. regia), were
inoculated each with six different wild-type Agrobacterium
strains. Poplar and wild cherry developed tumors that grew
hormone-independently, whereas on walnut, gall formation was
weak. On poplar and wild cherry, tumors induced by nopaline
strains developed spontaneously shoots that had a normal
phenotype and did not carry oncogenic T-DNA. From these
observations, we have established a co-inoculation method to
transform plants, using poplar as an experimental model. The
method is based on inoculation of stem internodes with an
Agrobacterium suspension containing both an oncogenic strain
that induces shoot differentiation and a disarmed strain that
provides the suitable genes in a binary vector. We used the
vector pBI121 carrying neo (kanamycin resistance) and uidA
(beta-glucuronidase) genes to facilitate early selection and
screening. Poplar plants derived from kanamycin-resistant
shoots that did not carry oncogenic T-DNA, were shown to
contain and to express neo and uidA genes. These results
suggest that wild-type Agrobacterium strains that induce shoot
formation directly from tumors can be used as a general tool
for gene transfer, avoiding difficult regeneration procedures.
9 NAL Call. No.: 450 P692
Anthocyanidins and flavonols, major nod gene inducers from
seeds of a black-seeded common bean (Phaseolus vulgaris L.).
Hungria, M.; Joseph, C.M.; Phillips, D.A.
Rockville, Md. : American Society of Plant Physiologists; 1991
Oct. Plant physiology v. 97 (2): p. 751-758; 1991 Oct.
Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Seed germination; Plant
composition; Anthocyanidins; Flavonoids; Nodulation;
Regulation; Rhizobium; Gene expression; Induction;
Transcription
Abstract: Eleven compounds released from germinating seeds of
a black-seeded bean (Phaseolus vulgaris L., cv PI165426CS)
induce transcription of nod genes in Rhizobium leguminosarum
biovar phaseoli. Aglycones from 10 of those compounds were
identified by spectroscopic methods (ultraviolet/visible,
proton nuclear magnetic resonance, and mass spectroscopy), and
their biological activities were demonstrated by induction of
beta-galactosidase activity in R. leguminosarum strains
containing nodA-lacZ or nodC-lacZ fusions controlled by R.
leguminosarum biovar phaseoli nodD genes. By making
comparisons with authentic standards, the chemical structures
for aglycones from the 10 molecules were confirmed as being
anthocyanidins (delphinidin, petunidin, and malvidin) and
flavonols (myricetin, quercetin, and kaempferol). All
anthocyanidins and flavonols had 3-O-glycosylation and free
hydroxyl groups at the 4', 5, and 7 positions. Hydrolysis
experiments showed that the mean concentration required for
half-maximum nod gene induction (I50) by the 10 glycosides was
about half that of the corresponding aglycones. The mean I50
value for the three anthocyanidins (360 nanomolar) was less (P
less than or equal to 0.05) than that of the three flavonol
aglycones (980 nanomolar). Each seed released approximately
2500 nanomoles of anthocyanidin and 450 nanomoles of flavonol
nod gene inducers in conjugated forms during the first 6 hours
of imbibition. Based on amounts and activities of the
compounds released, anthocyanins contributed approximately 10-
fold more total nod-inducing activity than flavonol
glycosides. These anthocyanidins from bean seeds represent the
first nod-inducing compounds identified from that group of
flavonoids.
10 NAL Call. No.: QK725.P532
An antisense gene stimulates ethylene hormone production
during tomaot fruit ripening.
Penarrubia, L.; Aguilar, M.; Margossian, L.; Fischer, R.L.
Rockville, Md. : American Society of Plant Physiologists; 1992
Jun. The Plant cell v. 4 (6): p. 681-687; 1992 Jun. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Antisense DNA;
Oxidoreductases; Plant proteins; Structural genes; Genetic
transformation; Transgenics; Gene expression; Ethylene
production; Fruits; Ripening
Abstract: The ripening of many fruits is controlled by an
increase in ethylene hormone concentration. E8 is a fruit
ripening protein that is related to the enzyme that catalyzes
the last step in the ethylene biosynthesis pathway, 1-
aminocyclopropane-1-carboxylic (ACC) oxidase. To determine the
function of E8, we have transformed tomato plants with an E8
antisense gene. We show here that the antisense gene inhibits
the accumulation of E8 protein during ripening. Whereas others
have shown that reduction of ACC oxidase results in reduced
levels of ethylene biosynthesis, we find that reduction of the
related E8 protein produces the opposite effect, an increase
in ethylene evolution specifically during the ripening of
detached fruit. Thus, E8 has a negative effect on ethylene
production in fruit.
11 NAL Call. No.: QK725.P532
An antisense pectin methylesterase gene alters pectin
chemistry and soluble solids in tomato fruit.
Tieman, D.M.; Harriman, R.W.; Ramamohan, G.; Handa, A.K.
Rockville, Md. : American Society of Plant Physiologists; 1992
Jun. The Plant cell v. 4 (6): p. 667-679; 1992 Jun. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Antisense DNA;
Pectinesterase; Structural genes; Genetic transformation;
Transgenics; Gene expression; Messenger RNA; Enzyme activity;
Fruits; Ripening; Pectins; Carbohydrate metabolism; Chemical
reactions; Polyuronides; Cell walls; Agronomic
characteristics; Inheritance
Abstract: Pectin methylesterase (PME, EC 3.1.11)
demethoxylates pectins and is believed to be involved in
degradation of pectic cell wall components by
polygalacturonase in ripening tomato fruit. We have introduced
antisense and sense chimeric PME genes into tomato to
elucidate the role of PME in fruit development and ripening.
Fruits from transgenic plants expressing high levels of
antisense PME RNA showed < 10% of wild-type PME enzyme
activity and undetectable levels of PME protein and mRNA.
Lower PME enzyme activity in fruits from transgenic plants was
associated with an increased molecular weight and
methylesterification of pectins and decreased levels of total
and chelator soluble polyuronides in cell walls. The fruits of
transgenic plants also contained higher levels of soluble
solids than wild-type fruits. This trait was maintained in
subsequent generations and segregated in normal Mendelian
fashion with the antisense PME gene. These results indicate
that reduction in PME enzyme activity in ripening tomato
fruits had a marked influence on fruit pectin metabolism and
increased the soluble solids content of fruits, but did not
interfere with the ripening process.
12 NAL Call. No.: 309.8 IN2
Antisense RNA keeps tomatoes green, mice in the pink.
Glanz, J.
Barrington, Ill. : Technical Pub. :.; 1992 Feb.
Research & development. p. 64-66; 1992 Feb.
Language: English
Descriptors: Lycopersicon esculentum; Antisense RNA; Gene
expression; Usda
13 NAL Call. No.: 450 P692
An Arabidopsis thaliana gene with sequence similarity to the
S-locus receptor kinase of Brassica oleracea--sequence and
expression.
Tobias, C.M.; Howlett, B.; Nasrallah, J.B.
Rockville, Md. : American Society of Plant Physiologists; 1992
May. Plant physiology v. 99 (1): p. 284-290; 1992 May.
Includes references.
Language: English
Descriptors: Arabidopsis thaliana; Genetic analysis; Genetic
code; Enzyme activity; Gene expression; Protein kinase;
Nucleotide sequences; Amino acid sequences
Abstract: Primary signal transduction plays a vital role in
the way plants react to environmental and developmental
signals. We report the sequence and expression of a putative
receptor kinase gene, ARK1, in Arabidopsis thaliana that may
be important in this regard. This Arabidopsis gene encodes a
transmembrane protein with a cytoplasmic kinase catalytic
domain, a transmembrane region, and an extracellular domain
with sequence similarity to the secreted S-locus glycoprotein
(SLG) gene of Brassica oleracea. This structure is similar to
the S-locus receptor kinase (SRK) gene of Brassica and to the
receptor kinase ZmPK1 gene of maize. RNA blots indicate that
transcripts accumulate predominantly in leaf tissue, with
limited amounts in stem and floral bud tissue and no
detectable transcripts accumulating in root tissue. A smaller
transcript that could be an alternative transcript of ARK1
also accumulates in leaf tissue. This transcript possibly
encodes a secreted SLG-like glycoprotein that lacks
transmembrane and kinase domains. The predominantly vegetative
expression of ARK1 indicates that this gene is not primarily
involved in pollen/pistil interactions in Arabidopsis.
14 NAL Call. No.: QK725.P54
Avocado fruit protoplasts: a cellular model system for
ripening studies. Percival, F.W.; Cass, L.G.; Bozak, K.R.;
Christoffersen, R.E. Berlin, W. Ger. : Springer International;
1991.
Plant cell reports v. 10 (10): p. 512-516; 1991. Includes
references.
Language: English
Descriptors: Persea Americana; Fruits; Protoplasts; Ripening;
Growth models; Protein synthesis; Genetic regulation; Gene
expression; Gene transfer
Abstract: Mesocarp protoplasts were isolated from mature
avocado fruits (Persea americana cv. Hass) at varying stages
of propylene-induced ripening. Qualitative changes in the
pattern of radiolabel incorporation into polypeptides were
observed in cells derived from fruit at the different stages.
Many of these differences correlate with those observed during
radiolabeling of polypeptides from fresh tissue slices
prepared from unripe and ripe fruit. Protoplasts isolated from
fruit treated with propylene for one day or more were shown to
synthesize cellulase (endo-beta-1,4-glucanase) antigen,
similar to the intact propylene-treated fruit. These results
suggest that the isolated protoplasts retain at least some
biochemical characteristics of the parent tissue. The cells
may also be used in transient gene expression assays.
Protoplasts isolated from preclimacteric and climacteric fruit
were equally competent in expressing a chimeric test gene,
composed of the CaMV 35S RNA promoter fused to the bacterial
chloramphenicol acetyltransferase gene, which was introduced
by electroporation.
15 NAL Call. No.: QK725.P532
Both internal and external regulatory elements control
expression of the pea fed-1 gene in transgenic tobacco
seedlings.
Gallo-Meagher, M.; Sowinski, D.A.; Elliott, R.C.; Thompson,
W.F. Rockville, Md. : American Society of Plant Physiologists;
1992 Apr. The Plant cell v. 4 (4): p. 389-395; 1992 Apr.
Includes references.
Language: English
Descriptors: Pisum sativum; Nicotiana tabacum; Controlling
elements; Gene expression; Ferredoxin; Structural genes;
Genetic regulation; Light; Etiolation; Transgenics; Genetic
transformation; Messenger RNA; Promoters; Leaves; Roots;
Seedlings
Abstract: In previous studies using leaves of light-grown
transgenic tobacco plants, we have shown that sequences
located within the transcribed region of the pea Fed-1 gene
(encoding ferredoxin 1) are major cis-acting determinants of
light-regulated mRNA accumulation. However, we show here that
these internal sequences are less important for the Fed-1
light response in etiolated tobacco seedlings than they are in
green leaves and that upstream elements confer organ
specificity and contribute significantly to Fed-1 light
responses in etiolated material. Light effects mediated by
upstream response elements are thus most pronounced during the
initial induction of gene activity, whereas internal elements
play a more prominent role in modulating Fed-1 expression once
the gene is already active.
16 NAL Call. No.: 75.8 P842
Breeding for 2N egg production in haploid X species 2X potato
hybrids. Ortiz, R.; Peloquin, S.J.
Orono, Me. : Potato Association of America; 1991 Oct.
American potato journal v. 68 (10): p. 691-703; 1991 Oct.
Includes references.
Language: English
Descriptors: Solanum tuberosum; Plant breeding; Interspecific
hybridization; Wild plants; Solanum; Solanum chacoense;
Hybrids; Haploids; Chromosome number; Ova; Diploidy;
Genotypes; Alleles; Meiosis; Mutants; Genetic regulation;
Recessive genes; Heritability; Overdominance; Linkage
disequilibrium; Expressivity; Gene expression; Quantitative
traits; Fruits; Seed set; Tubers; Crop quality; Recurrent
selection; Screening; Genotype environment interaction;
Genetic variation; Genetic variance
17 NAL Call. No.: SB732.6.M65
cDNA cloning, structure, and expression of a novel
pathogenesis-related protein in bean.
Sharma, Y.K.; Hinojos, C.M.; Mehdy, M.C.
St. Paul, Minn. : APS Press; 1992 Jan.
Molecular plant-microbe interactions : MPMI v. 5 (1): p.
89-95; 1992 Jan. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Colletotrichum
lindemuthianum; Host parasite relationships; Pathogenesis-
related proteins; Dna; Cloning; Genes; Gene expression;
Genetic analysis; Messenger RNA; Amino acid sequences;
Comparisons; Nucleotide sequences; Molecular biology
18 NAL Call. No.: QK725.P532
Cell-specific expression of plant histone H2A genes.
Koning, A.J.; Tanimoto, E.Y.; Kiehne, K.; Rost, T.; Comai, L.
Rockville, Md. : American Society of Plant Physiologists; 1991
Jul. The Plant cell v. 7 (3): p. 657-665; 1991 Jul. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Pisum sativum; Multiple
genes; Histones; Gene expression; Messenger RNA; Fruits;
Fruiting; Gynoecium; Buds; Axils; Root tips; Shoots; Apical
meristems; Root meristems; Cortex; Nucleotide sequences; Amino
acid sequences; Cell division; Genetic variation; Spatial
distribution
Abstract: Histone H2A is a component of eukaryotic chromatin
whose expression has not been studied in plants. We isolated
and characterized a tomato and a pea cDNA encoding histone
H2A. We found that in tomato H2A is encoded by a small gene
family and that both the pea and the tomato mRNAs are
polyadenylated. Tomato H2A has 82% amino acid residue identity
to pea H2A, 83% to wheat, and 65% to human and yeast H2A.
Plant H2As differ from fungal and animal H2As in their amino-
terminal and carboxy-terminal regions. Carboxy-terminal plant
H2A regions contain the motif SPKK, a peptide implicated in
binding of A/T-rich DNA regions. By using RNA gel blot
analysis, we determined that the steady-state mRNA level of
these genes was abundant in apices and early developing fruit
and very low in mature tissues. In situ RNA hybridization
showed strong spatial regulation because the mRNA was abundant
in some cells and not detectable in others. In tomato shoot
tips, H2A-expressing cells were distributed irregularly in or
near meristems. In tomato or pea root tips, expressing cells
were concentrated near the apex, and their distribution was
consistent with that expected of cycling cells. Other H2A
transcripts were found in nondividing cortical cells that are
known to undergo endoduplication during the late maturation
phase of primary development.
19 NAL Call. No.: QK725.P532
Cell-specific expression of the carrot EP2 lipid transfer
protein gene. Sterk, P.; Booij, H.; Schellekens, G.A.; Kammen,
A. van; Vries, S.C. de Rockville, Md. : American Society of
Plant Physiologists; 1991 Sep. The Plant cell v. 3 (9): p.
907-921; 1991 Sep. Includes references.
Language: English
Descriptors: Daucus carota; Genes; Plant proteins; Gene
expression; Messenger RNA; Nucleotide sequences; Amino acid
sequences; Embryogenesis; Plant embryos; Somatic
embryogenesis; Shoots; Apical meristems; Epidermis; Leaves;
Flowers; Seeds; Cell suspensions; Plant development
Abstract: A cDNA corresponding to a 10-kD protein, designated
extracellular protein 2 (EP2), that is secreted by embryogenic
cell cultures of carrot was obtained by expression screening.
The derived protein sequence and antisera against heterologous
plant lipid transfer proteins identified the EP2 protein as a
lipid transfer protein. Protein gel blot analysis showed that
the EP2 protein is present in cell walls and conditioned
medium of cell cultures. RNA gel blot analysis revealed that
the EP2 gene is expressed in embryogenic cell cultures, the
shoot apex of seedlings, developing flowers, and maturing
seeds. In situ hybridization showed expression of the EP2 gene
in protoderm cells of somatic and zygotic embryos and
transient expression in epidermis cells of leaf primordia and
all flower organs. In the shoot apical meristem, expression is
found in the tunica and lateral zone. In maturing seeds, the
EP2 gene is expressed in the outer epidermis of the
integument, the seed coat, and the pericarp epidermis, as well
as transiently in between both mericarps. Based on the
extracellular location of the EP2 protein and the expression
pattern of the encoding gene, we propose a role for plant
lipid transfer proteins in the transport of cutin monomers
through the extracellular matrix to sites of cutin synthesis.
20 NAL Call. No.: QK710.P62
Characterisation of a wound-induced transcript from the
monocat asparagus that shares similarity with a class of
intracellular pathogenesis-related (PR) proteins.
Warner, S.A.J.; Scott, R.; Draper, J.
Dordrecht : Kluwer Academic Publishers; 1992 Jul.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(4): p. 555-561; 1992 Jul. Includes references.
Language: English
Descriptors: Asparagus officinalis; Structural genes; Dna;
Pathogenesis-related proteins; Nucleotide sequences; Amino
acid sequences; Gene expression; Messenger RNA; Genetic
regulation; Abiotic injuries; Mechanical damage
Abstract: We report the isolation and characterisation of a
wound-induced cDNA designated AoPR1 from a suspension of
mesophyll cells that had been mechanically isolated from
cladodes of light-grown Asparagus officinalis seedlings by
grinding in a mortar and pestle. The transcript abundance is
up-regulated following cell separation and in chopped
mesocotyl tissue from dark-grown seedlings. The expression of
AoPR1 was shown by northern analysis to be located around the
site of damage. Sequence analysis revealed similarity between
the predicted AoPR1 polypeptide and bean PvPR1 and PvPR2
proteins, the potato pSTH2 protein, the pea PI49 protein, the
parsley PcPR1-1 protein and a major pollen allergen from birch
(BetvI). These transcripts have been shown to be induced in
response to microbial attack or fungal elicitation. To our
knowledge, this is the first example of a monocot cDNA
belonging to this class of intracellular pathogenesis-related
proteins (IPRs).
21 NAL Call. No.: QH442.A1G4
Characterization and evolution of napin-encoding genes in
radish and related crucifers.
Raynal, M.; Depigny, D.; Grellet, F.; Delseny, M.
Amsterdam : Elsevier Science Publishers; 1991.
Gene v. 99 (1): p. 77-86; 1991. Includes references.
Language: English
Descriptors: Raphanus sativus; Brassica napus var. oleifera;
Arabidopsis; Multigene families; Plant proteins; Cloning;
Nucleotide sequences; Amino acid sequences; Restriction
mapping; Evolution; Repetitive DNA; Messenger RNA; Gene
expression; Embryogenesis
Abstract: Three cDNA clones, encoding napin storage proteins
from radish, were isolated and sequenced. They fall into two
classes differing in the size of the primary translation
product. Sequences of the two classes are very well conserved
and they display an organization very similar to that of the
homologous genes from rapeseed and Arabidopsis which have
previously been described. On the basis of hybridization
intensity and the number of restriction fragments, we estimate
that the radish napin multigene family is represented by eight
to twelve members. The use of probes specific to each
subfamily demonstrates that they contribute to a similar
extent to the production of napin mRNA. Analysis of the
sequence data suggests that the napin ancestral genes are
probably derived from successive duplication and divergence of
a protogene. Comparing other available napin sequences with
those of radish reveals intriguing features. Comparison of the
coding sequences shows that the homology between the radish
and rapeseed sequences is much higher than that between each
of the four members of the Arabidopsis gene family. This would
suggest that the duplications which gave rise to the different
members occurred independently in the two groups of species
after separation of Arabidopsis from the Brassica lineage.
However, similar comparison carried out on the 3'-noncoding
sequences does not support this hypothesis, but shows that
slightly different duplicated genes probably already existed
in the common ancestor to the three genera. This paradox can
be resolved by assuming that, within each genus, coding
sequences for napin-encoding genes have been considerably
homogenized as a result of concerted evolution.
22 NAL Call. No.: SB732.6.M65
Characterization of a chimeric cauliflower mosaic virus
isolate that is more severe and accumulates to higher
concentrations than either of the strains from which it was
derived.
Anderson, E.J.; Trese, A.T.; Sehgal, O.P.; Schoelz, J.E.
St. Paul, Minn. : APS Press; 1992 Jan.
Molecular plant-microbe interactions : MPMI v. 5 (1): p.
48-54; 1992 Jan. Includes references.
Language: English
Descriptors: Brassica campestris var. rapa; Cauliflower mosaic
caulimovirus; Strains; Strain differences; Virulence;
Dwarfing; Symptoms; Chimeras; Phenotypes; Viral antigens;
Genes; Gene expression; Dna; Rna; Genetic analysis; Stability;
Synergism; Molecular biology
23 NAL Call. No.: SB732.6.M65
Characterization of a DNA region required for production of
the phytotoxin coronatine by Pseudomonas syringae pv. tomato.
Ma, S.W.; Morris, V.L.; Cuppels, D.A.
St. Paul, Minn. : APS Press; 1991 Jan.
Molecular plant-microbe interactions : MPMI v. 4 (1): p.
69-74; 1991 Jan. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Pseudomonas syringae pv.
tomato; Pathogenicity; Phytotoxins; Biosynthesis; Genetic
regulation; Genetic analysis; Dna; Insertional mutagenesis;
Mutants; Ice nucleation; Gene expression; Host parasite
relationships
24 NAL Call. No.: QK710.P68
Characterization of a shoot-specific, GA3- and ABA-regulated
gene from tomato. Shi, L.; Gast, R.T.; Gopalraj, M.;
Olszewski, N.E.
Oxford : Blackwell Scientific Publishers and BIOS Scientific
Publishers; 1992 Mar.
The plant journal v. 2 (2): p. 153-159; 1992 Mar. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Mutants; Gibberellic
acid; Abscisic acid; Rna; Genetic code; Genetic regulation;
Gene expression; Growth; Transcription; Nucleotide sequences;
Amino acid sequences
25 NAL Call. No.: QK710.P68
Characterization of cDNAs encoding two isoforms of granule-
bound starch synthase which show differential expression in
developing storage organs of pea and potato.
Dry, I.; Smith, A.; Edwards, A.; Bhattacharyya, M.; Dunn, P.;
Martin, C. Oxford : Blackwell Scientific Publishers and BIOS
Scientific Publishers; 1992 Mar.
The plant journal v. 2 (2): p. 193-202; 1992 Mar. Includes
references.
Language: English
Descriptors: Pisum sativum; Solanum tuberosum; Plant embryos;
Tubers; Plant composition; Developmental stages; Glycogen
(starch) synthase; Isoenzymes; Genetic code; Dna; Gene
expression; Amino acid sequences
26 NAL Call. No.: QH442.A1G4
Characterization of INF56, a gene expressed during infection
structure development of Uromyces appendiculatus.
Xuei, X.; Bhairi, S.; Staples, R.C.; Yoder, O.C.
Amsterdam : Elsevier Science Publishers; 1992.
Gene v. 110 (1): p. 49-55; 1992. Includes references.
Language: English
Descriptors: Uromyces appendiculatus; Genes; Introns;
Polypeptides; Nucleotide sequences; Amino acid sequences; Gene
expression; Messenger RNA; Hyphae; Cell differentiation;
Infections; Pathogenesis; Thigmotropism
Abstract: The bean rust fungus, Uromyces appetidiculatus,
undergoes thigmotropic differentiation to produce infection
structures. Six differentiation-specific genes have been
isolated and one, INF24, has been characterized [Bhairi et
al., Gene 81 (1989) 237-243]. Here, we report the structure of
a second gene, IVF56, which was subcloned on a 2.6-kb fragment
and sequenced. The location of the 1.0-kb INF56 transcript was
determined by S1 nuclease protection and primer extension. A
TATA box was found 38 bp upstream and a CAAT box 130 bp
upstream from the major transcription start point (tsp). The
gene contains two open reading frames: ORF2 is nested within
ORF1; they share a 67-bp intron. ORF1 encodes a 14.1-kDa
polypeptide which has an amino acid sequence rich in Gly, Pro
and Ser. It has sequence similarity to a functional domain
(V2) of mammalian cytokeratin type II. ORF2 encodes a 10.1-kDa
polypeptide which is rich in Pro. It shares similarity with
the cell-surface recognition region of chicken fibronectin.
Hybrid selection and in vitro translation of the INF56 mRNA
yielded two polypeptides of 15.5 and 23 kDa, as estimated by
sodium dodecyl sulfate-polyacrylamide-gel electrophoresis.
INF56 is constitutively expressed at a low level, but the
abundance of its steady-state transcript is upshifted 4.5 h
after spore hydration during the period that infection
structures are formed.
27 NAL Call. No.: QK710.P62
Characterization of the gene encoding the 10 kDa polypeptide
of photosystem II from Arabidopsis thaliana.
Gil-Gomez, G.; Marrero, P.F.; Haro, D.; Ayte, J.; Hegardt,
F.G. Dordrecht : Kluwer Academic Publishers; 1991 Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 517-522; 1991 Sep. Includes references.
Language: English
Descriptors: Arabidopsis thaliana; Genes; Polypeptides; Plant
proteins; Photosystem ii; Cloning; Nucleotide sequences; Amino
acid sequences; Restriction mapping; Gene expression; Genetic
regulation; Leaves; Stems; Light
Abstract: We report the characterization of a 1388 bp genomic
fragment from Arabidopsis thaliana that encompasses the entire
transcription unit of the gene encoding the precursor of 10
kDa polypeptide of photosystem II, 495 bp of the 5' flanking
region and 73 bp of the 3' boundary of the gene. The deduced
protein shows 78% and 73% homology, respectively, with its
homologues from potato and spinach. The transcription of the
gene seems to be greatly enhanced by light and only
transcribed in substantial amounts in leaves and stems.
Analysis of the putative 5' regulatory region of the gene
shows homology with several cis-elements involved in light
regulation of the transcription.
28 NAL Call. No.: 442.8 Z34
Characterization of the pea ENOD12B gene and expression
analyses of the two ENOD12 genes in nodule, stem and flower
tissue.
Govers, F.; Harmsen, H.; Heidstra, R.; Michielsen, P.; Prins,
M.; Kammen, A. van
Berlin, W. Ger. : Springer International; 1991 Aug.
M G G : Molecular and general genetics v. 228 (1/2): p.
160-166; 1991 Aug. Includes references.
Language: English
Descriptors: Pisum sativum; Multigene families; Plant
proteins; Proline; Cell wall components; Nucleotide sequences;
Amino acid sequences; Promoters; Transcription; Gene
expression; Messenger RNA; Root nodules; Stems; Flowers;
Rhizobium leguminosarum
Abstract: The ENOD12 gene family in pea consists of two
different members. The cDNA clone, pPsENOD12, represents the
PsENOD12A gene. The second ENOD12 gene, PsENOD12B, was
selected from a genomic library using pPsENOD12 as a probe and
this gene was sequenced and characterized. The coding regions
of the two genes are strikingly similar. Both encode proteins
having a signal peptide sequence and a region with
pentapeptide units rich in prolines. ENOD12A has a series of
rather conserved repeating pentapeptide units, whereas in
ENOD12B the number of pentapeptide units is less and these are
less conserved. From the amino acid sequence it is obvious
that the PsENOD12 genes encode proline-rich proteins which are
closely related to proteins that have been identified as
components of soybean cell walls (SbPRPs). Previously,
Northern blot analyses had shown that ENOD12 genes are
expressed in a tissue-specific manner. A high expression level
is found in Rhizobium-infected roots and in nodules, whereas
expression in flower and stem is lower. This raised the
question of which gene is expressed where and when. The
availability of the sequences of both ENOD12 genes allowed us
to analyse the expression of the two genes separately.
Specific oligonucleotides were used to copy the ENOD12 mRNAs
and to amplify the cDNAs in a polymerase chain reaction. It
was demonstrated that in all the tissues containing ENOD12
mRNA, both genes PsENOD12A and PsENOD12B are transcribed and
that the relative amounts of PsENOD12A and PsENOD12B mRNA
within each tissue are more or less equal. Moreover, the
expression pattern during infection and nodule development is
the same for the two genes. These results show that two
closely related genes have the same tissue-specific expression
pattern and that the gene that we have isolated is an actively
transcribed gene. The 2.7 kb genomic region that contains the
PsENOD12B gene has a 41 pb nearly direct repeat in the 5'
flanking region of the gene (between -1447 and -1153)
29 NAL Call. No.: QH506.E46
Chloroplast mRNA 3' end processing requires a nuclear-encoded
RNA-binding protein.
Schuster, G.; Gruissem, W.
Oxford, Eng. : IRL Press; 1991 Jun.
The EMBO journal - European Molecular Biology Organization v.
10 (6): p. 1493-1502; 1991 Jun. Includes references.
Language: English
Descriptors: Spinacia oleracea; Chloroplast genetics;
Messenger RNA; Degradation; Binding proteins; Cloning; Genes;
Nucleotide sequences; Amino acid sequences; Binding site; Gene
expression; Biological development; Chloroplasts
Abstract: The protein coding regions of plastid mRNAs in
higher plants are generally flanked by 3' inverted repeat
sequences. In spinach chloroplast mRNAs, these inverted repeat
sequences can fold into stem-loop structures and serve as
signals for the correct processing of the mature mRNA 3' ends.
The inverted repeat sequences are also required to stabilize
5' upstream mRNA segments, and interact with chloroplast
proteins in vitro. To dissect the molecular components
involved in chloroplast mRNA 3' end processing and stability,
a spinach chloroplast protein extract containing mRNA 3' end
processing activity was fractionated by FPLC and RNA affinity
chromatography. The purified fraction consisted of several
proteins and was capable of processing the 3' ends of the
psbA, rbcL, petD and rps14 mRNAs. This protein fraction was
enriched for a 28 kd RNA-binding protein (28RNP) which
interacts with both the precursor and mature 3' ends of the
four mRNAs. Using specific antibodies to this protein, the
poly(A) RNA-derived cDNA for the 28RNP was cloned and
sequenced. The predicted amino acid sequence for the 28RNP
reveals two conserved RNA-binding domains, including the
consensus sequences RNP-CS1 and CS2, and a novel acidic and
glycine-rich N-terminal domain. The accumulation of the
nuclear-encoded 28RNP mRNA and protein are developmentally
regulated in spinach cotyledons, leaves, root and stem, and
are enhanced during light-dependent chloroplast development.
The general correlation between accumulation of the 28RNP and
plastid mRNA during development, together with the result that
depletion of the 28RNP from the chloroplast protein extract
interferes with the correct 3' end processing of several
chloroplast mRNAs, suggests that the 28RNP is required for
plastid mRNA 3' end processing and/or stability.
30 NAL Call. No.: QK710.P62
Circadian oscillations of nuclear-encoded chloroplast proteins
in pea (Pisum sativum).
Adamska, I.; Scheel, B.; Kloppstech, K.
Dordrecht : Kluwer Academic Publishers; 1991 Nov.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(5): p. 1055-1065; 1991 Nov. Includes references.
Language: English
Descriptors: Pisum sativum; Gene expression; Transcription;
Chlorophyll a/b binding protein; Plant proteins; Chloroplasts;
Messenger RNA; Circadian rhythm; Diurnal variation;
Oscillation; Seedlings; Ribosomes; Nucleoproteins
Abstract: The diurnal and circadian expression of light-
inducible chloroplast proteins, i.e. light-harvesting
chlorophyll a/b protein (LHCP), early light-inducible protein
(ELIP) and Fe-S Rieske, has been studied in young pea
plantlets at the level of mRNA integrated into polysomal
complexes and at the level of proteins. Under light-dark as
well as constant light conditions the levels of the three
nuclear-encoded chloroplast proteins oscillate while the
investigated plastid-encoded proteins, large subunit of
ribulose-1,5-bisphosphate carboxylase (LSU), reaction center
protein D1 and cytochrome f, do not show oscillations at the
protein level. The levels of the nuclear-encoded polysome-
bound mRNAs fluctuate in parallel with the changes in the
levels of poly(A) RNA which were described previously. Under
constant light conditions the oscillation at the level of
polysomal bound mRNA is readily dampened while the steady-
state levels of the investigated nuclear-encoded proteins
still fluctuate. We conclude that the extent of expression of
the genes for the nuclear-encoded chloroplast proteins studied
is controlled by a circadian oscillator primarily, but not
exclusively, at the level of transcription.
31 NAL Call. No.: QK725.P532
cis-Element combinations determine phenylalanine ammonia-lyase
gene tissue-specific expression patterns.
Leyva, A.; Liang, X.; Pintor-Toro, J.A.; Dixon, R.A.; Lamb,
C.J. Rockville, Md. : American Society of Plant Physiologists;
1992 Mar. The Plant cell v. 4 (3): p. 263-271; 1992 Mar.
Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Nicotiana tabacum; Genes;
Promoters; Phenylalanine ammonia-lyase; Controlling elements;
Gene expression; Xylem; Transgenics; Genetic transformation;
Molecular mapping; Deletions; Phloem; Parenchyma; Mutants
Abstract: The bean phenylalanine ammonia-lyase gene 2 (PAL2)
is expressed in the early stages of vascular development at
the inception of xylem differentiation, associated with the
synthesis of lignin precursors. This is part of a complex
program of developmental expression regulating the synthesis
of functionally diverse phenylpropanoid natural products.
Analysis of the expression of PAL2 promoter-beta-glucuronidase
gene fusions in transgenic tobacco plants showed that
functionally redundant cis elements located between
nucleotides -289 and -74 relative to the transcription start
site were essential for xylem expression, but were not
involved in expression in leaf primordia and stem nodes or in
establishing tissue specificity in petals. The -135 to -119
region implicated in xylem expression contains a negative
element that suppresses the activity of a cryptic cis element
for phloem expression located between -480 and -289. The
functional properties of each vascular element are conserved
in stem, petiole, and root, even though the xylem and phloem
are organized in different patterns in these organs. We
conclude that the PAL2 promoter has a modular organization and
that tissue-specific expression in the vascular system
involves a negative combinatorial interaction, modulation of
which may provide a flexible mechanism for modification of
tissue specificity.
32 NAL Call. No.: QK710.P62
Cloning and characterization of a carrot hsp70 gene.
Lin, X.; Chern, M.S.; Zimmerman, J.L.
Dordrecht : Kluwer Academic Publishers; 1991 Dec.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(6): p. 1245-1249; 1991 Dec. Includes references.
Language: English
Descriptors: Daucus carota; Genes; Heat shock proteins;
Cloning; Nucleotide sequences; Amino acid sequences; Gene
expression; Messenger RNA
33 NAL Call. No.: QK710.P62
Cloning and characterization of a gene involved in phytoene
synthesis from tomato.
Ray, J.; Moureau, P.; Bird, C.; Bird, A.; Grierson, D.;
Maunders, M.; Truesdale, M.; Bramley, P.; Schuch, W.
Dordrecht : Kluwer Academic Publishers; 1992 Jun.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(3): p. 401-404; 1992 Jun. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Structural genes;
Pseudogenes; Ligases; Nucleotide sequences; Amino acid
sequences; Exons; Promoters; Fruits; Ripening; Gene
expression; Transcription; Messenger RNA
34 NAL Call. No.: 381 J824
Cloning and characterization of the P subunit of glycine
decarboxylase from pea (Pisum sativum).
Turner, S.R.; Ireland, R.; Rawsthorne, S.
Baltimore, Md. : American Society for Biochemistry and
Molecular Biology; 1992 Mar15.
The Journal of biological chemistry v. 267 (8): p. 5355-5360;
1992 Mar15. Includes references.
Language: English
Descriptors: Pisum sativum; Glycine; Carboxy-lyases;
Structural genes; Cloning; Gene expression; Multigene
families; Nucleotide sequences; Amino acid sequences
Abstract: A pea leaf cDNA library constructed in lambda gt11
was screened with an antibody raised to the P subunit of
glycine decarboxylase. One of the positive clones isolated was
sequenced and shown to contain an open reading frame, which
encoded the entire P subunit polypeptide. Aligning the deduced
amino acid sequence with the amino acid sequence determined
directly from the NH2 terminus of the mature P subunit shows
the presence of a putative 86 amino acid leader sequence,
presumably required for import into the mitochondria, and
gives a Mr of the mature protein of 105,000. Comparison of
this deduced amino acid sequence with the sequence of a
pyridoxal phosphate-containing peptide isolated from the P
subunit of chicken liver glycine decarboxylase shows
remarkable conservation. The P subunit, however, shows little
sequence homology with other published amino acid
decarboxylases. Expression of the P subunit mRNA shows a
pattern very similar to that of the corresponding polypeptide:
it is strongly light induced and is expressed at a much higher
level in leaves than in other tissues. Southern blot analysis
suggests that the P subunit is encoded by a small multigene
family.
35 NAL Call. No.: 442.8 Z34
Cloning and expression analysis of a potato cDNA that encodes
branching enzyme: evidence for co-expression of starch
biosynthetic genes. Kossmann, J.; Visser, R.G.F.; Muller-
Rober, B.; Willmitzer, L.; Sonnewald, U. Berlin, W. Ger. :
Springer International; 1991 Nov.
M G G : Molecular and general genetics v. 230 (1/2): p. 39-44;
1991 Nov. Includes references.
Language: English
Descriptors: Solanum tuberosum; Genes; Hexosyltransferases;
Cloning; Gene expression; Messenger RNA; Tubers;
Nucleotidyltransferases; Starch; Carbohydrate metabolism;
Amino acid sequences
Abstract: One of the key enzymes involved in the formation of
amylopectin, which is the major component of starch, is
branching enzyme. A cDNA for potato branching enzyme was
cloned by screening a tuber-specific cDNA expression library
using an antiserum directed against a denatured preparation of
the protein. Complementation of an Escherichia coli strain
deficient in branching enzyme was achieved using a construct
derived from this clone. Analysis of the expression of the
gene in potato revealed a close association with conditions
favouring starch biosynthesis. The expression pattern of the
gene coding for potato branching enzyme, as analyzed at the
mRNA level, closely resembles that of AGPase S, a gene coding
for one of the subunits of ADP-glucose pyrophosphorylase,
which is the key regulatory enzyme in the starch biosynthetic
pathway. This raises the possibility that enzymes involved in
the pathway are coordinately regulated at the transcriptional
level.
36 NAL Call. No.: 450 P693
Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate
synthase and expression of its mRNA in ripening apple fruit.
Dong, J.G.; Kim, W.T.; Yip, W.K.; Thompson, G.A.; Li, L.;
Bennett, A.B.; Yang, S.F.
Secaucus, N.J. : Springer-Verlag; 1991.
Planta v. 185 (1): p. 38-45; 1991. Includes references.
Language: English
Descriptors: Malus sylvestris; Apples; Fruits; Ripening;
Postharvest physiology; Genetic regulation; Dna; Cloning;
Genetic code; Acc; Ligases; Gene expression; Messenger RNA;
Restriction mapping; Nucleotide sequences; Amino acid
sequences
37 NAL Call. No.: QK725.P532
Control of ethylene synthesis by expression of a bacterial
enzyme in transgenic tomato plants.
Klee, H.J.; Hayford, M.B.; Kretzmer, K.A.; Barry, G.F.;
Kishore, G.M. Rockville, Md. : American Society of Plant
Physiologists; 1991 Nov. The Plant cell v. 3 (11): p.
1187-1193; 1991 Nov. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Pseudomonas; Genetic
transformation; Gene transfer; Transgenics; Hydrolases;
Cloning; Nucleotide sequences; Amino acid sequences; Gene
expression; Ethylene production; Leaves; Fruits; Ripening;
Ripening stage; Firmness
Abstract: Synthesis of the phytohormone ethylene is believed
to be essential for many plant developmental processes. The
control of ripening in climacteric fruits and vegetables is
among the best characterized of these processes. One approach
to reduce ethylene synthesis in plants is metabolism of its
immediate precursor, 1-aminocyclopropane-1-carboxylic acid
(ACC). Soil bacteria containing an enzyme, ACC deaminase, were
identified by their ability to grow on ACC as a sole nitrogen
source. The gene encoding ACC deaminase was cloned and
introduced into tomato plants. Reduction in ethylene synthesis
in transgenic plants did not cause any apparent vegetative
phenotypic abnormalities. However, fruits from these plants
exhibited significant delays in ripening, and the mature
fruits remained firm for at least 6 weeks longer than the
nontransgenic control fruit. These results indicated that ACC
deaminase is useful for examining the role of ethylene in many
developmental and stress-related processes in plants as well
as for extending the shelf life of fruits and vegetables whose
ripening is mediated by ethylene.
38 NAL Call. No.: 442.8 Z34
The coxII gene in carrot mitochondria contains two introns.
Lippok, B.; Brennicke, A.; Wissinger, B.
Berlin, W. Ger. : Springer International; 1992 Mar.
M G G : Molecular and general genetics v. 232 (2): p. 322-327;
1992 Mar. Includes references.
Language: English
Descriptors: Daucus carota; Mitochondrial DNA; Cytochrome-c
oxidase; Genes; Introns; Transcription; Messenger RNA; Gene
expression; Rna editing; Restriction mapping; Nucleotide
sequences; Dna conformation; Amino acid sequences
Abstract: The gene for cytochrome oxidase subunit II (coxII)
in carrot is encoded by a unique locus in the mitochondrial
genome. In contrast to the coxII genes in the numerous other
plant species investigated to date, the coding region is
interrupted by two group II introns. The carrot 5' intron is
the homologue of the single intervening sequence found in
several monocot and dicot coxII genes. Sequences similar to
the 3' intron of the carrot coxII gene have not been reported
previously and are not detectable by hybridization with
Oenothera mtDNA. Northern hybridizations indicate complex
precursor transcript patterns with mRNA molecules up to 10 kb
length. The excised intron sequences appear to be stably
maintained in the mRNA pool. Amino acid sequence comparisons
suggest that the carrot coxII mRNA needs to be edited by
numerous C to U transitions.
39 NAL Call. No.: 442.8 Z34
Cytochrome c1 from potato: a protein with a presequence for
targeting to the mitochondrial intermembrane space.
Braun, H.P.; Emmermann, M.; Kruft, V.; Schmitz, U.K.
Berlin, W. Ger. : Springer International; 1992 Jan.
M G G : Molecular and general genetics v. 231. (2): p.
217-225; 1992 Jan. Includes references.
Language: English
Descriptors: Solanum tuberosum; Genes; Cytochrome c;
Nucleotide sequences; Amino acid sequences; Transcription;
Gene expression; Messenger RNA; Precursors; Protein
transport; Mitochondria; Membranes
Abstract: Here we report the primary structure of potato
cytochrome c1, a nuclear-encoded subunit of complex III. Using
heterologous antibodies directed against cytochrome c1 from
yeast two types of clones were isolated from an expression
library, suggesting that at least two different genes are
present and expressed in the genome. Northern blot analysis
reveals that slightly varying levels of cytochrome c1
transcripts are present in all potato tissues analysed. A 1304
bp insert of one of the cDNA clones (pC13II) encodes the
entire 320 amino acids of the precursor protein corresponding
to a molecular weight of 35.2 kDa. As revealed by direct amino
acid sequence determination of the cytochrome c1 protein
another cDNA clone (pC18I) encodes the major form of
cytochrome c1 present in potato tuber mitochondria. Western
blots of subfractionated potato mitochondria show that the
mature protein present in the membrane fraction is smaller
than the pC13II encoded protein synthesized in Escherichia
coli. The transient presequence of the protein is 77 amino
acids long and has a bipartite polarity profile characteristic
of presequences involved in targeting to the intermembrane
space of fungal mitochondria. It consists of a positively
charged NH2-terminal part which resembles "matrix targeting
domains" and an adjacent hydrophobic region showing sequence
similarities to "intramitochondrial sorting domains". The
amino-terminal region of potato cytochrome c1 is the first
presequence of a plant protein of the mitochondrial
intermembrane space to be determined and may be useful in the
study of intramitochondrial sorting in plants.
40 NAL Call. No.: 450 P692
Deletion mutants of chlorophyll a/b binding proteins are
efficiently imported into chloroplasts but do not integrate
into thylakoid membranes. Huang, L.; Adam, Z.; Hoffman, N.E.
Rockville, Md. : American Society of Plant Physiologists; 1992
May. Plant physiology v. 99 (1): p. 247-255; 1992 May.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Mutants; Chloroplasts;
Thylakoids; Translocation; Chlorophyll a/b binding protein;
Genetic regulation; Gene expression
Abstract: Chlorophyll a/b binding polypeptides (CABp) are
integral thylakoid membrane proteins containing three
membrane-spanning helices. We have created a series of
mutations in tomato CABp to test whether individual membrane
helices with hydrophilic flanking sequences, when fused to a
transit peptide, can be imported into chloroplasts and
correctly targeted to thylakoid membranes. All of the mutated
precursors, including those with large C-terminal and internal
deletions, were imported successfully, showing that these
regions of the mature CABp are not required for import into
chloroplasts. All mutants tested, containing either one or two
membrane helices, were found primarily in the stroma and not
in the thylakoids. The small amount of protein found
associated with the thylakoids was largely resistant to alkali
extraction but was sensitive to protease, unlike wild-type
protein, which is resistant to both treatments. When incubated
with thylakoids in the absence of stroma and/or ATP, a
significant amount of wild-type protein assumes a form that is
resistant to alkali extraction but is protease sensitive, like
the imported deletion proteins. This form of the wild-type
protein is not chased into a protease-resistant form by adding
stroma and/or ATP. These results suggest that CABp can
spontaneously associate with membranes as an aberrant species
that is not an intermediate in the process of integration. The
inability of the deletion forms of CABp to assume a protease-
resistant conformation suggests that correct integration is
afforded by elements within the entire protein that
collectively contribute to the proper conformation of the
protein. The ability of deletion mutants to associate with
thylakoids in a nonphysiological way suggests that the study
of such mutants may not be useful in elucidating thylakoid-
targeting signals.
41 NAL Call. No.: QK710.P62
A detailed study of the regulation and evolution of the two
classes of patatin genes in Solanum tuberosum L.
Lin, X.Y.; Rocha-Sosa, M.; Hummel, S.; Willmitzer, L.;
Frommer, W.B. Dordrecht : Kluwer Academic Publishers; 1991
Dec.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(6): p. 1139-1154; 1991 Dec. Includes references.
Language: English
Descriptors: Solanum tuberosum; Multigene families; Plant
proteins; Tubers; Nucleotide sequences; Promoters; Chimeras;
Beta-glucuronidase; Reporter genes; Gene expression;
Histoenzymology; Genetic transformation; Agrobacterium
tumefaciens; Genetic regulation; Evolution; Leaves;
Transgenics
Abstract: The class-specific expression of patatin genes was
investigated by analysing four new patatin genes. A class I
patatin gene from cv. Berolina as well as a class I and two
class II patatin genes from the monohaploid cultivar AM
80/5793 were isolated and partially sequenced. Sequence
comparison indicates rearrangements as the major source for
the generation of diversity between the different members of
the classes. The expression of single genes was studied in
potato plants transformed with chimaeric genes where the
putative patatin promoters were fused to the GUS reporter
gene. A detailed histochemical analysis reveals that both
class I genes are expressed as the previously described class
I patatin gene B33 from cv. Berolina, i.e. in the starch-
containing cells of potato tubers and in sucrose-induced
leaves. The class II gene pgT12 shows the same pattern as the
previously described class II gene pgT2, i.e. expression in
root tips and in the vascular tissue of tubers, whereas no
activity was detectable for pgT4. Thus the expression pattern
of both classes of genes seems to be stable at least within or
even between different cultivars.
42 NAL Call. No.: 442.8 Z34
Determination of steady-state mRNA levels of individual
chlorophyll a/b binding protein genes of the tomato cab gene
family.
Piechulla, B.; Kellmann, J.W.; Pichersky, E.; Schwartz, E.;
Forster, H.H. Berlin, W. Ger. : Springer International; 1991
Dec01.
M G G : Molecular and general genetics v. 230 (3): p. 413-422;
1991 Dec01. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Multigene families;
Chlorophyll a/b binding protein; Gene expression;
Transcription; Messenger RNA; Promoters; Nucleotide
sequences; Repetitive DNA
Abstract: The steady-state levels of mRNA produced by 14
genes encoding members of the tomato chlorophyll a/b binding
protein family were quantified. All genes were found to be
expressed in leaf tissue, but the mRNAs accumulated to
significantly different levels. The transcripts of cab 1A, cab
1B, cab 3A and cab 3B, encoding the Type I LHC proteins of
photosystem II, are abundant, while low levels were measured
for mRNAs encoding the Type II LHC II and the LHC I proteins.
Sequences from the 5' upstream regions (-400 to translational
start) of some cab genes were determined in this study, and a
total of 16 tomato cab gene promoters for which sequences are
now available were analyzed. Significant sequence conservation
was found for those genes which are tandemly linked on the
chromosome. However, the level of sequence conservation is
different for the different cab subfamilies, e.g. 85%
similarity between cab 1A and cab 1 D vs. 45% sequence
similarity between cab 3A and cab 3C upstream sequences.
Characteristic GATA repeats with a conserved spacing were
found in 5' upstream sequences of cab 1 A-D, cab 3 A-C, cab 11
and cab 12. The consensus sequence CCTTATCAT, which is
believed to mediate light responsiveness, was found at
different locations in the upstream sequences of cab 6B, cab
7, cab 8, cab 9, cab 10A, cab 10B and cab 11. In 11 out of 15
genes the transcription initiation site was found to center on
the triplet TCA.
43 NAL Call. No.: QK725.P532
Developmental and organ-specific changes in promoter DNA-
protein interactions in the tomato rbcS gene family.
Manzara, T.; Carrasco, P.; Gruissem, W.
Rockville, Md. : American Society of Plant Physiologists; 1991
Dec. The Plant cell v. 3 (12): p. 1305-1316; 1991 Dec.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Multigene families;
Promoters; Ribulose-bisphosphate carboxylase; Dna binding
proteins; Binding site; Nucleotide sequences; Dna
footprinting; Gene expression; Transcription; Plant
development; Fruit; Leaves; Cotyledons; Light; Etiolation
Abstract: The five genes encoding ribulose-1,5-bisphosphate
carboxylase (rbcS) from tomato are differentially expressed.
Transcription of the genes is organ specific and
developmentally regulated in fruit and light regulated in
cotyledons and leaves. DNase I footprinting assays were used
to map multiple sites of DNA-protein interaction in the
promoter regions of all five genes and to determine whether
the differential transcriptional activity of each gene
correlated with developmental or organ-specific changes in
DNA-protein interactions. We show organ-specific differences
in DNase I protection patterns, suggesting that differential
transcription of rbcS genes is controlled at least in part at
the level of DNA-protein interactions. In contrast, no changes
were detected in the DNase I footprint pattern generated with
nuclear extracts from dark-grown cotyledons versus cotyledons
exposed to light, implying that light-dependent regulation of
rbcS transcription is controlled by protein-protein
interactions or modification of DNA binding proteins. During
development of tomato fruit, most DNA-protein interactions in
the rbcS promoter regions disappear, coincident with the
transcriptional inactivation of the rbcS genes. In nuclear
extracts from nonphotosynthetic roots and red fruit, the only
detectable DNase I protection corresponds to a G-box binding
activity. Detection of other DNA binding proteins in extracts
from these organs and expression of nonphotosynthetic genes
exclude the possibility that roots and red fruit are
transcriptionally inactive. The absence of complex promoter
protection patterns in these organs suggests either that
cooperative interactions between different DNA binding
proteins are necessary to form functional transcription
complexes or that there is developmental and organ-specific
regulation of several rbcS-specific transcription factors in
these organs. The DNase I-protected DNA sequences defined in
this study are discussed in the context of conserved DNA
44 NAL Call. No.: QK725.P532
Developmental and pathogen-induced activation of the
Arabidopsis acidic chitinase promoter.
Samac, D.A.; Shah, D.M.
Rockville, Md. : American Society of Plant Physiologists; 1991
Oct. The Plant cell v. 3 (10): p. 1063-1072; 1991 Oct.
Includes references.
Language: English
Descriptors: Arabidopsis thaliana; Lycopersicon esculentum;
Alternaria solani; Phytophthora infestans; Chitinase;
Promoters; Beta-glucuronidase; Reporter genes; Chimeras; Gene
expression; Leaves; Infections; Histoenzymology; Transgenics;
Genetic transformation; Ethylene; Salicylic acid; Roots
Abstract: Expression of the Arabidopsis acidic chitinase
promoter was investigated during plant development and in
response to inoculation with fungal pathogens. A chimeric gene
composed of 1129 bp of 5' upstream sequence from the acidic
chitinase gene was fused to the beta-glucuronidase (GUS)
coding region and used to transform Arabidopsis and tomato.
Promoter activity was monitored by histochemical and
quantitative assays of GUS activity. In healthy transgenic
plants, the acidic chitinase promoter activity was restricted
to roots, leaf vascular tissue, hydathodes, guard cells, and
anthers, whereas GUS expression was induced in mesophyll cells
surrounding lesions caused by Rhizoctonia solani infection of
transgenic Arabidopsis. In transgenic tomato plants, GUS
expression was induced around necrotic lesions caused by
Alternaria solani and Phytophthora infestans. Expression of
the acidic chitinase promoter-GUS transgene was weakly induced
by infiltrating leaves with salicylic acid. Analysis of a
series of 5' deletions of the acidic chitinase promoter in
Arabidopsis indicated that the proximal 192 bp from the
transcription initiation site was sufficient to establish both
the constitutive and induced pattern of expression. Elements
further upstream were involved in quantitative expression of
the gene. The location of a negative regulatory element was
indicated between -384 and -590 and positive regulatory
elements between -1129 and-590.
45 NAL Call. No.: 381 J824
Differential expression within a three-gene subfamily encoding
a plasma membrane H+-ATPase in Nicotiana plumbaginifolia.
Perez, C.; Michelet, B.; Ferrant, V.; Bogaerts, P.; Boutry, M.
Baltimore, Md. : American Society for Biochemistry and
Molecular Biology; 1992 Jan15.
The Journal of biological chemistry v. 267 (2): p. 1204-1211;
1992 Jan15. Includes references.
Language: English
Descriptors: Nicotiana plumbaginifolia; Plasma membranes;
Adenosinetriphosphatase; Multigene families; Gene expression;
Genetic regulation; Nucleotide sequences; Amino acid sequences
Abstract: Genomic and cDNA clones for the three members of a
gene subfamily (pma) encoding a plasma membrane H+-
translocating ATPase in Nicotiana plumbaginifolia were
isolated and sequenced. They are between 95 and 96% identical
at the deduced amino acid sequence level. Sequence comparisons
with the corresponding tomato genes (Ewing, N. N., Wimmers, L.
E., Meyer, D. J., Chetelat, R. T., and Bennett, A. B. (1990)
Plant Physiol. 94, 1874-1881) indicate that divergence among
the three N. plumbaginifolia pma genes occurred before the
development of the Solanaceae family. Here, determination of
pma1 transcription initiation sites reveals several 5'
boundaries located 266 to 120 nucleotides upstream from the
plasma membrane H+-ATPase translation initiation codon. The
5'-untranslated region contains a small open reading frame, 9
residues long. pma3 has a single, 264-nucleotide long 5'
leader containing a 5-residue open reading frame. The latter
is completely conserved in a corresponding tomato gene. These
features suggest the possibility of translational regulation
of plant pma genes. S1 nuclease protection assays on total
cellular RNA isolated from different organs reveals that all
three genes are expressed in leaf, stem, flower, and root
tissues, albeit at different levels according to the organ and
gene. The different genes for the plant H+-translocating
ATPase are thus subject to differential regulation of
transcription, possibly related to specific aspects of enzyme
function.
46 NAL Call. No.: 500 N21P
Differential induction of 3-deoxy-D-arabino-heptulosonate 7-
phosphate synthase genes in Arabidopsis thaliana by wounding
and pathogenic attack. Keith, B.; Dong, X.; Ausubel, F.M.;
Fink, G.R.
Washington, D.C. : The Academy; 1991 Oct01.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (19): p. 8821-8825; 1991 Oct01.
Includes references.
Language: English
Descriptors: Arabidopsis thaliana; Amino acid sequences; Amino
acids; Biosynthesis; Dna; Gene expression; Genetic code;
Injuries; Lyases; Microbial proteins; Mutations; Nucleotide
sequences; Peptides; Pseudomonas syringae
Abstract: We have isolated cDNAs from two distinct genes
encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)
synthase (EC 4.1.2.15) in Arabidopsis thaliana. Predicted
protein sequences from both genes, DHS1 and DHS2, and a potato
DAHP synthase gene are highly related, but none shows
significant sequence similarity to conserved microbial DAHP
synthase proteins. Despite this structural difference, the
DHS1 cDNA complements mutations in a yeast strain lacking DAHP
synthase activity. DHS1 RNA levels increase in Arabidopsis
leaves subjected either to physical wounding or to
infiltration with pathogenic Pseudomonas syringae strains.
DHS2 RNA levels are not increased by these treatments,
suggesting that the DHS1 and DHS2 proteins fulfill different
physiological functions. Other enzymes in the Arabidopsis
aromatic pathway are also encoded by duplicated genes, an
arrangement that may allow independent regulation of aromatic
amino acid biosynthesis by distinct physiological requirements
such as protein synthesis and secondary metabolism. The
presence of amino-terminal extensions characteristic of
chloroplast transit peptides on DHS1 and DHS2 suggests that
both proteins may be targeted to the chloroplast.
47 NAL Call. No.: QK710.P62
Direct gene transfer into Actinidia deliciosa protoplasts:
analysis of transient expression of the CAT gene using TLC
autoradiography and a GC-MS-based method.
Oliveira, M.M.; Barroso, J.; Pais, M.S.S.
Dordrecht : Kluwer Academic Publishers; 1991 Aug.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(2): p. 235-242; 1991 Aug. Includes references.
Language: English
Descriptors: Actinidia deliciosa; Genetic transformation;
Direct DNAuptake; Protoplasts; Polyethylene glycol; Gene
transfer; Gene expression; Reporter genes; Chloramphenicol
acetyltransferase; Autoradiography; Thin layer chromatography;
Gas chromatography; Mass spectrometry
Abstract: Chloramphenicol acetyl transferase (CAT) gene was
used as a reporter gene to assess the conditions for
polyethylene glycol (PEG)-mediated transfection of kiwifruit
protoplasts. The effect of plasmid concentration and the
presence of carrier DNA were each assessed by analysing CAT
activity in transfected protoplasts using thin-layer
chromatography (TLC) autoradiographic detection of acetylated
chloramphenicol. A gas chromatography (GC) and gas
chromatography-mass spectrometry (GC-MS) non-radioactive
method was developed for monitoring CAT gene activity. This
method provides a high speed of analysis (30 min) and precise
means of detecting acetylated products at the nanomolar level,
enabling quantification at very low transfection rates. Using
this method we optimized plasmid and PEG concentration and
also assessed the effect of heat shock on transfection. The
best CAT activity was obtained using 30% polyethylene glycol
4000 and by submitting protoplasts to heat shock (45 degrees
C, 5 min) prior to transfection.
48 NAL Call. No.: QH573.N37
Dissection of the light-responsive elements of pea rbcS3A.
Gilmartin, P.M.; Memelink, J.; Chua, N.H.
Berlin, W. Ger. : Springer-Verlag; 1991.
NATO ASI series : Series H : Cell biology v. 50: p. 141-155;
1991. In the series analytic: Phytochrome properties and
biological action / edited by B. Thomas and C.B. Johnson.
Proceedings of the NATO Advanced Research Workshop on
Phytochrome Properties and Biological Action, July 22-27,
1990, Chichester, UK. Includes references.
Language: English
Descriptors: Pisum sativum; Genes; Ribulose-bisphosphate
carboxylase; Promoters; Gene expression; Transcription;
Genetic regulation; Light; Phytochrome; Dna binding proteins;
Controlling elements; Binding site
49 NAL Call. No.: QK710.P62
DNA sequence of the tomato fruit expressed proline-rich
protein gene TPRP-F1 reveals an intron within the 3
untranslated transcript.
Salts, Y.; Kenigsbuch, D.; Wachs, R.; Gruissem, W.; Barg, R.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 407-409; 1992 Jan. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Plant proteins;
Proline; Amino acid sequences; Nucleotide sequences; Fruits;
Gene expression; Messenger RNA
50 NAL Call. No.: SB732.6.M65
Effects of flavonoids released naturally from bean (Phaseolus
vulgaris) on nodD-regulated gene transcription in Rhizobium
leguminosarum bv. phaseoli. Hungria, M.; Johnston, A.W.B.;
Phillips, D.A.
St. Paul, Minn. : APS Press; 1992 May.
Molecular plant-microbe interactions : MPMI v. 5 (3): p.
199-203; 1992 May. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Symbionts; Interactions;
Rhizobium leguminosarum; Root exudates; Seeds; Flavonols;
Anthocyanins; Anthocyanidins; Flavonoids; Strains;
Transcription; Induction; Genistein; Gene expression;
Molecular biology
51 NAL Call. No.: QH442.B5
Engineered resistance to tomato spotted wilt virus, a
negative-strand RNA virus.
Gielen, J.J.L.; Haan, P. de; Kool, A.J.; Peters, D.; Grinsven,
M.Q.J.M. van; Goldbach, R.W.
New York, N.Y. : Nature Publishing Company; 1991 Dec.
Bio/technology v. 9 (12): p. 1363-1367; 1991 Dec. Includes
references.
Language: English
Descriptors: Nicotiana tabacum; Tomato spotted wilt virus;
Genetic transformation; Gene transfer; Viral proteins; Genes;
Gene expression; Transgenics; Genetic resistance
52 NAL Call. No.: QK710.P62
An ethylene-related cDNA from ripening apples.
Ross, G.S.; Knighton, M.L.; Lay-Yee, M.
Dordrecht : Kluwer Academic Publishers; 1992 May.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(2): p. 231-238; 1992 May. Includes references.
Language: English
Descriptors: Malus pumila; Dna; Messenger RNA; Genes;
Cloning; Acc; Oxidoreductases; Nucleotide sequences; Amino
acid sequences; Gene expression; Fruits; Ripening; Ethylene
production; Abiotic injuries
Abstract: We report the isolation of a ripening-related apple
cDNA which is complementary to a mRNA which may be involved in
ethylene production. Poly(A)+ RNA was extracted from cortical
tissue of ripe apple fruit (Malus domestica Borkh cv. Golden
Delicious) and a cDNA library constructed in the plasmid
vector pSPORT. The library was screened with pTOM13, a tomato
cDNA clone thought to code for ACC oxidase in that fruit. An
apple cDNA clone (pAP4) was isolated and sequenced. The 1182
bp cDNA insert includes an open reading frame of 942 bp, and
shows strong homology with reported tomato and avocado
sequences, both at the nucleic acid and amino acid levels. The
polypeptide has a calculated molecular mass of 35.4 kDa and a
calculated pI of 5.15. In apple cortical tissue, expression of
pAP4-complementary RNA increased with ethylene production by
the fruit during ripening. Expression was also enhanced in
both ethylene-treated and wounded fruit.
53 NAL Call. No.: QH506.E46
Exonic sequences are required for elicitor and light
activation of a plant defense gene, but promoter sequences are
sufficient for tissue specific expression.
Douglas, C.J.; Hauffe, K.D.; Ites-Morales, M.E.; Ellard, M.;
Paszkowski, U.; Hahlbrock, K.; Dangl, J.L.
Oxford, Eng. : IRL Press; 1991 Jul.
The EMBO journal - European Molecular Biology Organization v.
10 (7): p. 1767-1775; 1991 Jul. Includes references.
Language: English
Descriptors: Petroselinum crispum; Nicotiana tabacum; Genes;
Ligases; Promoters; Exons; Beta-glucuronidase; Reporter genes;
Gene expression; Genetic regulation; Phytophthora megasperma;
Cell wall components; Transgenics; Genetic transformation;
Ultraviolet radiation; Abiotic injuries; Defense mechanisms
Abstract: The parsley 4CL-1 gene encodes 4-coumarate:CoA
ligase, a key enzyme of general phenylpropanoid metabolism. As
well as being transcriptionally activated by such stresses as
pathogen infection, UV-irradiation, and wounding, expression
of 4CL-1 is developmentally regulated. In this paper we
present evidence that 4CL-1 cis-acting elements which control
stress-induced and developmental expression are physically
separated. The ability of a series of 4CL gene constructions
to respond to elicitor and light in stably or transiently
transformed parsley cells was tested. While inducible
expression was observed from all templates in which the 4CL-1
structural gene was fused to the 4CL-1 promoter, fusions of
the promoter to the GUS reporter gene were completely
unresponsive. The element(s) required for responsiveness
appear to be exonic, since 4CL-1 introns and 3' flanking DNA
had no effect on inducibility. Furthermore, this
unconventional regulatory mode operates in transgenic tobacco
plants, where we show that a 4CL-1 promoter fragment specifies
correct cell-specific expression when fused to GUS yet is
unresponsive to elicitor and light.
54 NAL Call. No.: QP501.B642
Expression and molecular cloning of drought-induced genes in
the wild tomato Lycopersicon chilense.
Chen, R.D.; Tabaeizadeh, Z.
Ottawa : National Research Council of Canada; 1992 Mar.
Biochemistry and cell biology; Biochimie et biologie
cellulaire v. 70 (3/4): p. 199-206; 1992 Mar. Includes
references.
Language: English
Descriptors: Lycopersicon; Leaves; Drought resistance; Water
stress; Heat shock; Abscisic acid; Protein synthesis;
Messenger RNA; Genes; Clones; Gene expression
55 NAL Call. No.: QK710.P62
Expression and stability of amplified genes encoding
5-enolpyruvylshikimate-3-phosphate synthase in glyphosate-
tolerant tobacco cells.
Wang, Y.; Jones, J.D.; Weller, S.C.; Goldsbrough, P.B.
Dordrecht : Kluwer Academic Publishers; 1991 Dec.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(6): p. 1127-1138; 1991 Dec. Includes references.
Language: English
Descriptors: Nicotiana tabacum; Genes; Ligases; Nucleotide
sequences; Amino acid sequences; Amplification; Glyphosate;
Herbicide resistance; Gene expression; Messenger RNA; Cell
lines; Regeneration
Abstract: Two distinct cDNAs for 5-enolpyruvylshikimate-3-
phosphate synthase (EPSPS) were obtained from a glyphosate-
tolerant tobacco cell line. The cDNAs were 89% identical and
the predicted sequences of the mature proteins were greater
than 83% identical with EPSPS proteins from other plants.
Tobacco EPSPS proteins were more similar to those from tomato
and petunia than Arabidopsis. One cDNA clone, EPSPS-1,
represented a gene that was amplified in glyphosate-tolerant
cells, while the gene for EPSPS-2 was unaltered in these
cells. Consequently, EPSPS-1 mRNA was more abundant in
tolerant than unselected cells, whereas EPSPS-2 mRNA was at
relatively constant levels in these cell lines. Exposure of
unselected cells and tobacco leaves to glyphosate produced a
transient increase in EPSPS mRNA. However, glyphosate-tolerant
cells containing amplified copies of EPSPS genes did not show
a similar response following exposure to glyphosate. A
significant proportion of the EPSPS gene amplification was
maintained when tolerant cells were grown in the absence of
glyphosate for eight months. Plants regenerated from these
cells also contained amplified EPSPS genes.
56 NAL Call. No.: QK725.P532
Expression dynamics of the tomato rbcS gene family during
development. Wanner, L.A.; Gruissem, W.
Rockville, Md. : American Society of Plant Physiologists; 1991
Dec. The Plant cell v. 3 (12): p. 1289-1303; 1991 Dec.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Multigene families;
Ribulose-bisphosphate carboxylase; Gene expression;
Transcription; Messenger RNA; Genetic regulation; Leaves;
Fruits; Plant development; Cotyledons; Light; Etiolation
Abstract: The tomato rbcS gene family is composed of five
genes (rbcS1, 2, 3A, 3B, and 3C) that are differentially
expressed during tomato development. Nuclear run-on
transcription assays and RNA analysis were used to determine
the contribution of transcriptional and post-transcriptional
regulation to the accumulation of mRNA from the five rbcS
genes in tomato seedlings, leaves, and fruit. We found that
the qualitative pattern of mRNA accumulation is regulated at
the transcriptional level and that, in general, there is a
correlation of rates of rbcS transcription with overall rbcS
mRNA abundance in fruit and leaves. Although transcriptional
control is a primary determinant for rbcS gene expression in
tomato, examination of relative transcription rates and mRNA
accumulation of each rbcS gene demonstrated that there is also
significant post-transcriptional control of rbcS gene
expression during organ development. Individual rbcS mRNAs,
which have highly conserved coding sequences and differ only
in their 5' and 3' untranslated sequences, have different
stabilities. We showed that both transcription and stability
of individual rbcS mRNAs are altered in different organs and
by the developmental program within these organs as well as by
exposure to light. Together, the results provide a
comprehensive analysis of the extent of transcriptional and
post-transcriptional control that operates within the rbcS
gene family during plant development.
57 NAL Call. No.: 381 B523
Expression in Escherichia coli of UDP-glucose
pyrophosphorylase cDNA from potato tuber and functional
assessment of the five lysyl residues located at the
substrate-binding site.
Katsube, T.; Kazuta, Y.; Tanizawa, K.; Fukui, T.
Washington, D.C. : American Chemical Society; 1991 Sep03.
Biochemistry v. 30 (35): p. 8546-8551; 1991 Sep03. Includes
references.
Language: English
Descriptors: Solanum tuberosum; Udp; Glucose;
Nucleotidyltransferases; Vectors; Dna; Gene expression;
Cloning; Escherichia coli; Lysine; Binding site
Abstract: The entire structural gene for potato tuber UDP-
glucose pyrophosphorylase has been amplified from its cDNA by
the polymerase chain reaction and inserted into the expression
plasmid pTV118-N downstream from the lac promoter. Escherichia
coli JM105 cells carrying thus constructed plasmid produced
the enzyme to a level of about 5% of the total soluble protein
upon induction with isopropyl beta-D-thiogalactopyranoside.
The recombinant enzyme purified to homogeneity in two column
chromatographic steps was structurally and catalytically
identical with the enzyme purified from potato tuber except
for the absence of an N-terminal-blocking acetyl group. To
examine functional roles of the five lysyl residues that had
been identified by affinity labeling studies to be located at
or near the active site of the enzyme [Kazuta, Y., Omura, Y.,
Tagaya, M., Nakano, K., & Fukui, T. (1991) Biochemistry
(preceding paper in this issue)], they were replaced
individually by glutamine via site-directed mutagenesis. The
Lys-367 leads to Gln mutant enzyme was almost completely
inactive, and the Lys-263 leads to Gln mutant enzyme had
significantly decreased Vmax values with perturbed Km values
for pyrophosphate and alpha-D-glucose l-phosphate. Lys-329
leads to Gln also exhibited increased Km values for these
substrates but exhibited Vmax values similar to those of the
wild-type enzyme. The two mutant enzymes Lys-409 leads to Gln
and Lys-410 leads to Gln showed catalytic properties almost
identical with those of the wild-type enzyme. Thus, among the
five lysyl residues, Lys-367 is essential for catalytic
activity of the enzyme and Lys-263 and Lys-329 may participate
in binding of pyrophosphate and/or alpha-D-glucose l-
phosphate.
58 NAL Call. No.: QK710.P62
Expression of a bacterial lysine decarboxylase gene and
transport of the protein into chloroplasts of transgenic
tobacco.
Herminghaus, S.; Schreier, P.H.; McCarthy, J.E.G.; Landsmann,
J.; Botterman, J.; Berlin, J.
Dordrecht : Kluwer Academic Publishers; 1991 Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 475-486; 1991 Sep. Includes references.
Language: English
Descriptors: Nicotiana tabacum; Hafnia alvei; Agrobacterium
tumefaciens; Genetic transformation; Transgenics; Carboxy-
lyases; Genes; Gene expression; Promoters; Protein transport;
Chloroplasts; Cloning; Enzyme activity; Cadaverine;
Biosynthesis; Ribulose-bisphosphate carboxylase
Abstract: A possible approach for altering alkaloid
biosynthesis in plants is the expression of genes encoding key
enzymes of a pathway such as lysine decarboxylase (ldc) in
transgenic plants. Two strategies were followed here: one
focused on expression of the gene in the cytoplasm, the other
on subsequent targeting of the protein to the chloroplasts.
The ldc gene from Hafnia alvei was therefore (a) placed under
the control of the 1' promoter of the bidirectional Tr
promoter from Agrobacterium tumefaciens Ti- plasmid, and (b)
cloned behind the rbcS promoter from potato fused to the
coding region of the rbcS transit peptide, Both ldc
constructs, introduced into Nicotiana tabacum with the aid of
A. tumefaciens, were integrated into the plant genome and
transcribed as shown by Southern and northern hybridization.
However, LDC activity was only detectable in plants expressing
mRNA under the control of the rbcS promoter directing the LDC
fusion protein into chloroplasts with the aid of the transit
peptide domain. In plants expressing the processed bacterial
enzyme cadaverine levels increased from nearly zero to 0.3-1%
of dry mass.
59 NAL Call. No.: 450 P692
Expression of a Brassica napus malate synthase gene in
transgenic tomato plants during the transition from late
embryogeny to germination. Comai, L.; Matsudaira, K.L.;
Heupel, R.C.; Dietrich, R.A.; Harada, J.J. Rockville, Md. :
American Society of Plant Physiologists; 1992 Jan. Plant
physiology v. 98 (1): p. 53-61; 1992 Jan. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Brassica napus;
Agrobacterium tumefaciens; Genetic transformation;
Transgenics; Gene expression; Malic acid; Ligases; Plant
embryos; Genetic regulation; Genetic code; Nucleotide
sequences; Embryogenesis; Germination
Abstract: To study gene regulation during the transition from
late embryogeny to germination, we have analyzed the
expression of a gene encoding the glyoxylate cycle enzyme
malate synthase in transgenic tomato (Lycopersicon esculentum)
plants. We have shown that although there are at least four
classes of malate synthase genes in Brassica napus L., one
gene is expressed at a high level during both late embryogeny
and postgermination. Analyses of transgenic tomato plants
containing the expressed B. napus gene along with 4.7 and 1.0
kilobase pairs of 5' and 3' flanking sequences, respectively,
confirmed that a single gene is expressed at both stages of
development. Furthermore, localization studies have shown that
mRNA encoded by the B. napus gene is distributed throughout
the tissues of a mature embryo but is not detected in the
vascular cylinder of a seedling. We conclude that the
sequences required to qualitatively regulate the gene
correctly over the plant life cycle are present within the
transferred gene and/or flanking regions. Moreover, the malate
synthase gene is regulated differently during late embryogeny
and postgermination in the developing vascular cylinder.
60 NAL Call. No.: QK710.P62
Expression of a chimaeric granule-bound starch synthase-GUS
gene in transgenic potato plants.
Visser, R.G.F.; Stolte, A.; Jacobsen, E.
Dordrecht : Kluwer Academic Publishers; 1991 Oct.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(4): p. 691-699; 1991 Oct. Includes references.
Language: English
Descriptors: Solanum tuberosum; Agrobacterium tumefaciens;
Genetic transformation; Transgenics; Glycogen (starch)
synthase; Genes; Beta-glucuronidase; Reporter genes; Chimeras;
Starch granules; Gene expression; Tubers; Stolons; Leaves;
Enzyme activity; Histoenzymology; Sucrose; Sugars
Abstract: Granule-bound starch synthase is the key enzyme in
amylose synthesis. The regulation of this gene was
investigated using a chimaeric gene consisting of a 0.8 kb 5'
upstream sequence of the granule-bound starch synthase gene
from potato and the beta-glucuronidase gene which was
introduced into potato using an Agrobacterium tumefaciens
binary vector system. The chimaeric gene was highly expressed
in stolons and tubers, whereas the expression in leaves, stems
or roots from greenhouse-grown plants was relatively low.
However, leaves from in vitro grown plantlets exhibited an
elevated GUS expression. The expression of the chimaeric gene
was inducible in leaves by growth on relatively high
concentrations of sucrose, fructose and glucose and was about
30- to 50-fold higher than in leaves from greenhouse-grown
plants. The granule-bound starch synthase gene is expressed
organ-specifically since stolons and tubers showed GUS
activities 125- to 3350-fold higher than in leaves. The
activities in these two organs are 3- to 25-fold higher than
the expression of the CaMV-GUS gene. Histochemical analysis of
different tissues showed that only certain regions of leaves
and roots express high GUS activities. Stolons and tubers show
high expression.
61 NAL Call. No.: 450 P692
Expression of a conserved family of cytoplasmic low molecular
weight heat shock proteins during heat stress and recovery.
DeRocher, A.E.; Helm, K.W.; Lauzon, L.M.; Vierling, E.
Rockville, Md. : American Society of Plant Physiologists; 1991
Aug. Plant physiology v. 96 (4): p. 1038-1047; 1991 Aug.
Includes references.
Language: English
Descriptors: Pisum sativum; Heat stress; Stress response; Heat
shock proteins; Protein synthesis; Molecular weight; Messenger
RNA; Gene expression; Genetic regulation
Abstract: Plants synthesize several families of low molecular
weight (LMW) heat shock proteins (HSPs) in response to
elevated temperatures. We have characterized two cDNAs,
HSP18.1 and HSP17.9, that encode members of the class I family
of LMW HSPs from pea (Pisum sativum). In addition, we
investigated the expression of these HSPs at the mRNA and
protein levels during heat stress and recovery. HSP18.1 and
HSP17.9 are 82.1% identical at the amino acid level and are
80.8 to 92.9% identical to class I LMW HSPs of other
angiosperms. Heat stress experiments were performed using
intact seedlings subjected to a gradual temperature increase
and held at a maximum temperature of 30 to 42 degrees Celsius
for 4 hours. HSP18.1 and HSP17.9 mRNA levels peaked at the
beginning of the maximum temperature period and declined
rapidly after the stress period. Antiserum against a HSP18.1
fusion protein recognized both HSP18.1 and HSP17.9 but not
members of other families of LMW HSPs. The accumulation of
HSP18.1-immunodetected protein was proportional to the
severity of the heat stress, and the protein had a half-life
of 37.7 +/- 8 hours. The long half-life of these proteins
supports the hypothesis that they are involved in establishing
thermotolerance.
62 NAL Call. No.: QK725.P532
Expression of a maize sucrose phosphate synthase in tomato
alters leaf carbohydrate partitioning.
Worrell, A.C.; Bruneau, J.M.; Summerfelt, K.; Boersig, M.;
Voelker, T.A. Rockville, Md. : American Society of Plant
Physiologists; 1991 Oct. The Plant cell v. 3 (10): p.
1121-1130; 1991 Oct. Includes references.
Language: English
Descriptors: Zea mays; Lycopersicon esculentum; Genes;
Acyltransferases; Nucleotide sequences; Amino acid sequences;
Genetic transformation; Transgenics; Gene expression; Enzyme
activity; Starch; Sucrose; Carbohydrate metabolism; Leaves
Abstract: We isolated a complementary DNA sequence for the
enzyme sucrose phosphate synthase (SPS) from maize utilizing a
limited amino acid sequence. The 3509-bp cDNA encodes a 1068-
amino acid polypeptide. The identity of the cDNA was confirmed
by the ability of the cloned sequence to direct sucrose
phosphate synthesis in Escherichia coli. Because no plant-
specific factors were necessary for enzymatic activity, we can
conclude that SPS enzyme activity is conferred by a single
gene product. Sequence comparisons showed that SPS is
distantly related to the enzyme sucrose synthase. When
expressed from a ribulose bisphosphate carboxylase small
subunit promoter in transgenic tomatoes, total SPS activity
was boosted up to sixfold in leaves and appeared to be
physiologically uncoupled from the tomato regulation
mechanism. The elevated SPS activity caused a reduction of
starch and increase of sucrose in the tomato leaves. This
result clearly demonstrates that SPS is involved in the
regulation of carbon partitioning in the leaves.
63 NAL Call. No.: QK725.P532
Expression of amino-terminal portions of full-length viral
replicase genes in transgenic plants confers resistance to
potato virus X infection. Braun, C.J.; Hemenway, C.L.
Rockville, Md. : American Society of Plant Physiologists; 1992
Jun. The Plant cell v. 4 (6): p. 735-744; 1992 Jun. Includes
references.
Language: English
Descriptors: Nicotiana tabacum; Potato x potexvirus; Genetic
transformation; Transgenics; Rna polymerase; Structural genes;
Gene expression; Genetic resistance
Abstract: The first open reading frame (ORF 1) of potato
virus X (PVX) encodes a putative replicase gene. Transgenic
tobacco lines expressing ORF 1 are resistant to PVX infection
when inoculated with either PVX or PVX RNA. Analyses of lines
containing various portions of the ORF 1 gene demonstrated
that resistance is conferred to plants by expressing
approximately the first half of the ORF 1 gene. One line
expressing the untranslated leader and first 674 codons of ORF
1 is highly resistant to PVX infection. Conversely, lines
expressing either approximately the third or fourth quarter of
the ORF 1 gene, which contain the conserved nucleotide
triphosphate (NTP) binding motif and Gly-Asp-Asp (GDD) motif,
respectively, are not protected from PVX infection. In the
resistant full-length and amino-terminal lines, lower numbers
of local lesions were observed, and the virus accumulation in
the inoculated and upper leaves was reduced when compared with
the nontransformed control. When the performance of the most
resistant ORF 1 line was compared with the most resistant coat
protein (CP) line in a resistance test, the best ORF 1 line
was more resistant to PVX infection than the best transgenic
line expressing the PVX CP gene. These findings define a
promising new approach for controlling plant viral infection.
64 NAL Call. No.: 500 N21P
Expression of an antisense viral gene in transgenic tobacco
confers resistance to the DNA virus tomato golden mosaic
virus.
Day, A.G.; Bejarano, E.R.; Buck, K.W.; Burrell, M.;
Lichtenstein, C.P. Washington, D.C. : The Academy; 1991 Aug01.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (15): p. 6721-6725; 1991 Aug01.
Includes references.
Language: English
Descriptors: Nicotiana tabacum; Lines; Transgenics; Gene
expression; Genetic resistance; Genetic transformation;
Symptoms; Tomato golden mosaic geminivirus
Abstract: Transgenic tobacco plants carrying a genetic
cassette including an antisense DNA sequence of the virally
encoded AL1 gene of the geminivirus tomato golden mosaic virus
(TGMV) were constructed; AL1 encodes a protein absolutely
required for TGMV DNA replication. These genetic cassettes
also contained, on the same transcription unit, a gene
encoding hygromycin resistance, which allowed selection for
concomitant expression of the antisense gene. In transgenic
lines, RNA transcripts of the predicted size and strand
specificity were detected in antisense plants and sense
controls. After infection of plants with TGMV, by
agroinoculation, the frequency of symptom development was very
significantly reduced in a number of antisense lines and
correlated, broadly, with the abundance of antisense RNA
transcript and with a reduction in viral DNA harvested from
infected leaf tissue. We used an in vitro assay to study viral
DNA replication in the absence of cell-to-cell spread; no
replication was seen in five of the six antisense lines
studied, in contrast to controls.
65 NAL Call. No.: QK710.P62
Expression of antifreeze proteins in transgenic plants.
Hightower, R.; Baden, C.; Penzes, E.; Lund, P.; Dunsmuir, P.
Dordrecht : Kluwer Academic Publishers; 1991 Nov.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(5): p. 1013-1021; 1991 Nov. Includes references.
Language: English
Descriptors: Nicotiana tabacum; Lycopersicon esculentum;
Genetic transformation; Transgenics; Pseudopleuronectes; Blood
proteins; Genes; Gene expression; Messenger RNA;
Transcription; Recrystallization; Inhibition; Leaves; Ice
damage
Abstract: The quality of frozen fruits and vegetables can be
compromised by the damaging effects of ice crystal growth
within the frozen tissue. Antifreeze proteins in the blood of
some polar fishes have been shown to inhibit ice
recrystallization at low concentrations. In order to determine
whether expression of genes of this type confers improved
freezing properties to plant tissue, we have produced
transgenic tobacco and tomato plants which express genes
encoding antifreeze proteins. The afa3 antifreeze gene was
expressed at high steady-state mRNA levels in leaves from
transformed plants, but we did not detect inhibition of ice
recrystallization in tissue extracts. However, both mRNA and
fusion proteins were detectable in transgenic tomato tissue
containing a chimeric gene encoding a fusion protein between
truncated staphylococcal protein A and antifreeze protein.
Furthermore, ice recrystallization inhibition was detected in
this transgenic tissue.
66 NAL Call. No.: 464.8 P56
Expression of coat protein gene from cucumber mosaic virus
strain C in tobacco: protection against infections by CMV
strains transmitted mechanically or by aphids.
Quemada, H.D.; Gonsalves, D.; Slightom, J.L.
St. Paul, Minn. : American Phytopathological Society; 1991
Jul. Phytopathology v. 81 (7): p. 794-802; 1991 Jul. Includes
references.
Language: English
Descriptors: Nicotiana tabacum; Cucumber mosaic cucumovirus;
Strains; Strain differences; Coat proteins; Genes; Gene
transfer; Plasmids; Transgenics; Genetic transformation; Gene
expression; Disease resistance; Mechanical transmission;
Disease vectors; Myzus persicae
Abstract: The coat protein (CP) gene from cucumber mosaic
virus (CMV) strain C was engineered for expression in plants
and transferred into the genome of tobacco (Nicotiana tabacum
'Xanthi'). Transfer of the CP gene was confirmed, and plants
containing it produced the expected 1,400-nucleotide mRNA and
24-kDa protein products, which were detected by northern and
western blots, respectively. Transgenic tobacco plant lines
were infected with CMV strains C and Chi of subgroup I and
strain WL of subgroup II, transmitted mechanically or by
aphids. The effectiveness of the protection varied in
different transgenic plant lines, ranging from almost complete
protection to none, depending upon the challenge strain. These
experiments demonstrate that within a group of transgenic
plants expressing the CP gene of CMV strain C (subgroup I),
plant lines can be found that show a significant degree of
protection when challenged with CMV strains of either
subgroup.
67 NAL Call. No.: SB599.P45
Expression of disease resistance response genes in near-
isogenic pea cultivars following challenge by Fusarium
oxysporum race 1.
Hadwiger, L.A.; Chiang, C.C.; Horovitz, D.
London : Academic Press; 1992 Apr.
Physiological and molecular plant pathology v. 40 (4): p.
259-269; 1992 Apr. Includes references.
Language: English
Descriptors: Pisum sativum; Fusarium oxysporum f.sp. pisi;
Disease resistance; Genetic resistance; Cultivars; Lines; Gene
expression; Dominance; Genes; Varietal susceptibility; Races;
Host parasite relationships
Abstract: Previous research on the pea/Fusarium oxysporum
system has shown that the internal invasion of tap roots and
hypocotyls was less frequent in the cultivar Vantage, which
possesses a single dominant gene for resistance to Race 1,
than in the cultivar M410 which is susceptible. We monitored
these cultivar tissues for the expression of disease
resistance response genes 49 and 206, previously associated
with the expression of non-host resistance, in peas grown in
soil naturally infested with Fusarium oxysporum f. sp. pisi
(Race 1). The accumulation of distinct RNA products homologous
with both genes was evident in the resistant cultivar in a
period prior to and during the onset of wilt symptoms in the
susceptible cultivar. Additional periods of RNA accumulation
occurred in older flowering seedlings of both cultivars. These
were not gene-specific RNA accumulations and were probably
unrelated to resistance. Thus these response genes may
contribute to normal cellular functions which are also
utilized in the disease resistance response. The biochemical
functions of genes 49 and 206 remain unknown.
68 NAL Call. No.: 448.3 J82
Expression of Erwinia amylovora hrp genes in response to
environmental stimuli.
Wei, Z.M.; Sneath, B.J.; Beer, S.V.
Washington, D.C. : American Society for Microbiology; 1992
Mar. Journal of bacteriology v. 174 (6): p. 1875-1882; 1992
Mar. Includes references.
Language: English
Descriptors: Erwinia amylovora; Genes; Gene expression;
Genetic regulation; Transcription; Ph; Temperature; Ammonium;
Nicotinic acid; Nitrogen; Amino acids; Mannitol; Fructose;
Glycerol; Sucrose; Glucose; Maltose
Abstract: Seven hrp loci that are essential for the
hypersensitive reaction elicited by Erwinia amylovora were
transcriptionally fused with a derivative of transposon Tn5,
containing the promoterless Escherichia coli beta-
glucuronidase reporter gene. The seven hrp fusions were used
to monitor expression of the hrp loci in vitro and in planta.
No significant expression was detected in rich medium for any
of the fusions. However, five of them were expressed highly in
planta and in inducing medium that contains mannitol, salts,
and 5 mM (NH4)2SO4. Expression of these five hrp loci is
regulated by ammonium, nicotinic acid, complex-nitrogen
sources, certain carbon sources, temperature, and pH. Under
well-defined conditions, i.e., in inducing medium, no specific
plant components were required for transcriptional activation
of the hrp loci. The high levels of expression detected in
vitro were comparable to those determined during the
development of the hypersensitive reaction in tobacco.
Differential levels of expression of the hrp loci occurred in
host and nonhost plants. In pear, a host plant, expression of
the hrp loci was delayed and greatly reduced compared with
expression in tobacco leaves, a nonhost.
69 NAL Call. No.: 450 J8224
Expression of nuclear and chloroplast photosynthesis-specific
genes during leaf senescence.
Bate, N.J.; Rothstein, S.J.; Thompson, J.E.
Oxford : Oxford University Press; 1991 Jun.
Journal of experimental botany v. 42 (239): p. 801-811; 1991
Jun. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Gene expression; Genetic
regulation; Leaves; Senescence; Genes; Ribulose-bisphosphate
carboxylase; Ribosomal RNA; Ribosomal DNA; Photosystem ii;
Plant proteins; Light harvesting complexes; Messenger RNA;
Nuclei; Chloroplasts; Chloroplast genetics; Protein synthesis
Abstract: During senescence of the primary leaf of bean
(Phaseolus vulgaris L. cv. Kinghorn), total RNA declines by
approximately 10-fold, soluble protein declines by
approximately 3-fold and there is a decline in photosynthetic
capability. Pulse-labelling studies with 35S-methionine have
indicated that there is also a decline in synthesis of both
nuclear- and chloroplast-encoded photosynthetic proteins,
specifically the D-1 protein of Photosystem II (PSII) and the
ribulose 1,5 bisphosphate carboxylase/oxygenase (RubisCO)
large subunit (LSU), which are chloroplast-encoded, and the 26
kD light harvesting chlorophyll binding protein (LHCP) and
RubisCO small subunit (SSU), which are nuclear-encoded. Dot
blot and Northern blot hybridization studies with gene-
specific probes have indicated that transcript levels for the
chloroplast genes RRN, psbA and rbcL, which encode chloroplast
rRNA, the D-1 protein of PSII and LSU, respectively, remain a
constant proportion of total RNA throughout senescence. By
contrast, transcript levels for cab and rbcS, which are
nuclear genes encoding the 26 kD protein of LHCP and SSU,
respectively, comprise a progressively decreasing proportion
of total RNA as senescence progresses, whereas the transcript
for peroxidase, a non-photosynthetic nuclear-encoded protein,
remains a constant proportion of total RNA over the same
period. The data suggest that nuclear photosynthetic genes and
chloroplast genes are differentially regulated in senescing
leaves and follow patterns of expression similar to those
observed at other stages of development.
70 NAL Call. No.: QK725.P54
Expression of PVX coat protein gene under the control of
extensin-gene promoter confers virus resistance on transgenic
potato plants. Feher, A.; Skryabin, K.G.; Balazs, E.;
Preiszner, J.; Shulga, O.A.; Zakharyev, V.M.; Dudits, D.
Berlin, W. Ger. : Springer International; 1992.
Plant cell reports v. 11 (1): p. 48-52; 1992. Includes
references.
Language: English
Descriptors: Solanum tuberosum; Potato x potexvirus; Plant
breeding; Disease resistance; Agrobacterium tumefaciens;
Genetic transformation; Gene transfer; Gene expression;
Chimeras; Coat proteins; Genetic code
Abstract: Tuber discs of potato (Solanum tuberosum L.)
cultivars Desiree and Gracia were infected by Agrobacterium
tumefaciens carrying a binary vector with the coat protein
gene of potato virus X controlled by the carrot extensin gene
long-transcript promoter. Several transgenic potato plants
have been obtained by direct regeneration of shoots on culture
medium with kanamycin used for selection. The presence of the
coat protein gene was proved by Southern hybridization in
several transformants. Its low but detectable expression level
was shown by Northern and Western analysis. Ethephon treatment
resulted in a five-fold increase in the amounts of the coat
protein mRNA. The majority of transformants exhibited reduced
accumulation of virus RNA in inoculated leaves. Potentials in
the use of an ethylene-inducible promoter in the production of
virus-resistant transgenic plants will be discussed.
71 NAL Call. No.: QK827.S48
Expression of S-locus glycoprotein genes from Brassica
oleracea and B. campestris in transgenic plants of self-
compatible B. napus cv Westar. Nishio, T.; Toriyama, K.; Sato,
T.; Kandasamy, M.K.; Paolillo, D.J.; Nasrallah, J.B.;
Nasrallah, M.E.
Heidelberg : Springer International; 1992.
Sexual plant reproduction v. 5 (2): p. 101-109; 1992.
Includes references.
Language: English
Descriptors: Brassica oleracea; Brassica campestris; Brassica
napus; Agrobacterium tumefaciens; Genetic transformation;
Transgenics; Gene expression; Self compatibility; Self
incompatibility; Glycoproteins; Protein synthesis; Genetic
regulation; Immunocytochemistry; Cell ultrastructure; Spatial
distribution; Genes
72 NAL Call. No.: 381 B523
Expression of spinach glycolate oxidase in Saccharomyces
cerevisiae: purification and characterization.
Macheroux, P.; Massey, V.; Thiele, D.J.; Volokita, M.
Washington, D.C. : American Chemical Society; 1991 May07.
Biochemistry v. 30 (18): p. 4612-4619; 1991 May07. Includes
references.
Language: English
Descriptors: Spinacia oleracea; Saccharomyces cerevisiae;
(s)-2-hydroxy-acid oxidase; Purification; Plasmids; Gene
expression
Abstract: Glycolate oxidase from spinach has been expressed
in Saccharomyces cerevisiae. The active enzyme was purified to
near-homogeneity (purification factor approximately 1400-fold)
by means of hydroxyapatite and anion-exchange chromatography.
The purified glycolate oxidase is nonfluorescent and has
absorbance peaks at 448 (epsilon = 9200 M-1 cm-1) and 346 nm
in 0.1 M phosphate buffer, pH 8.3. The large bathochromic
shift of the near-UV band indicates that the N(3) position is
deprotonated at pH 8.3. A pH titration revealed that the pK of
the N(3) is shifted from 10.3 in free flavin to 6.4 in
glycolate oxidase. Glycolate oxidase is competitively
inhibited by oxalate with a Kd of 0.24 mM at 4 degrees C in
0.1 M phosphate buffer, pH 8.3. Three pieces of evidence
demonstrate that glycolate oxidase stabilizes a negative
charge at the N(1)-C(2 equal to O) locus: the enzyme forms a
tight sulfite complex with a Kd of 2.7 X 10(-7) M and
stabilizes the anionic flavosemiquinone and the benzoquinoid
form of 8-mercapto-FMN. Steady-state analysis at pH 8.3, 4
degrees C, yielded a Km = 1 X 10(-3) M for glycolate and Km =
2.1 X 10(-4) M for oxygen. The turnover number has been
determined to be 20 s-1. Stopped-flow studies of the reductive
(k = 25 s-1) and oxidative (k = 8.5 X 10(4) M-1 s-1) half-
reactions have identified the reduction of glycolate oxidase
to be the rate-limiting step.
73 NAL Call. No.: 448.3 J82
Expression of the avirulence gene avrBs3 from Xanthomonas
campestris pv. vesicatoria is not under the control of hrp
genes and is independent of plant factors.
Knoop, V.; Staskawicz, B.; Bonas, U.
Washington, D.C. : American Society for Microbiology; 1991
Nov. Journal of bacteriology v. 173 (22): p. 7142-7150; 1991
Nov. Includes references.
Language: English
Descriptors: Xanthomonas campestris pv. vesicatoria; Genes;
Gene expression; Plasmids; Capsicum annuum; Genetic regulation
Abstract: The avirulence gene avrBs3 from Xanthomonas
campestris pv. vesicatoria pepper race 1 is responsible for
the induction of a race-specific hypersensitive reaction in
resistant pepper cultivars. A DNA region of 3.7 kb, containing
several open reading frames and an internal repetitive region,
was shown previously to be necessary for avirulence activity
(U. Bonas, R. E. Stall, and B. Staskawicz, Mol. Gen. Genet.
218:127-136, 1989). The promoter of avrBs3 was identified by
using gene fusions to beta-glucuronidase. Also, we mapped the
transcription start site and showed that the avrBs3 gene is
expressed constitutively in cells grown in minimal or complex
medium and in planta. Polyclonal antibodies raised against a
fusion protein produced in Escherichia coli allowed the
identification of a 122-kDa protein in X. campestris pv.
vesicatoria cells expressing the avrBs3 gene. The antibody is
specific for AvrBs3 in X. campestris pv. vesicatoria cells but
also recognizes homologous proteins in other pathovars of X.
campestris. We found that AvrBs3 is localized intracellularly
in X. campestris pv. vesicatoria and is mainly in the soluble
fraction. The effect of mutations in the hrp gene cluster on
the function of AvrBs3 was examined. Expression of AvrBs3 in
X. campestris pv. vesicatoria grown in minimal or complex
medium is independent of the hrp gene cluster that determines
pathogenicity and hypersensitivity to X. campestris pv.
vesicatoria. In the plant, however, the hrp genes are required
for elicitation of a race-specific resistance response.
74 NAL Call. No.: QK710.P62
Expression of the potato leafroll luteovirus coat protein gene
in transgenic potato plants inhibits viral infection.
Wilk, F. van der; Willink, D.P.L.; Huisman, M.J.; Huttinga,
H.; Goldbach, R. Dordrecht : Kluwer Academic Publishers; 1991
Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 431-439; 1991 Sep. Includes references.
Language: English
Descriptors: Solanum tuberosum; Potato leaf roll luteovirus;
Genetic transformation; Transgenics; Coat proteins; Genes;
Cloning; Gene expression; Genetic resistance; Replication;
Disease transmission; Myzus persicae
Abstract: Transgenic potato plants, cultivar Desiree, were
produced that contained the coat protein gene of potato
leafroll luteovirus (PLRV). The transformed potato plants
expressed the PLRV coat protein (CP) RNA sequences but
accumulation of coat protein in transgenic tissues could not
be detected. Upon inoculation with PLRV, the PLRV CP RNA
expressing potato plants showed a reduced rate of virus
multiplication.
75 NAL Call. No.: 381 J824
Expression of the two isoforms of spinach ribulose 1,5-
bisphosphate carboxylase activase and essentially of the
conserved lysine in the consensus nucleotide-binding domain.
Shen, J.B.; Orozco, E.M. Jr; Ogren, W.L.
Baltimore, Md. : American Society for Biochemistry and
Molecular Biology; 1991 May15.
The Journal of biological chemistry v. 266 (14): p. 8963-8968;
1991 May15. Includes references.
Language: English
Descriptors: Spinacia oleracea; Ribulose-bisphosphate
carboxylase; Isoenzymes; Enzyme activity; Gene expression;
Vectors; Atp; Binding site; Lysine
Abstract: The two isoforms of ribulose 1,2-bisphosphate
carboxylase activase (Rbu-P2 carboxylase) from spinach
(Spinacea oleracea L.) were individually purified from
Escherichia coli transformed with expression vectors for the
appropriate cDNAs. Both isoforms catalyzed activation of Rbu-
P2 Carboxylase (ribulose 1, 5-bis-phosphate
carboxylase/oxygenase, EC 4.1.1.39) and ATP hydrolysis. The
kinetics of the two isoforms with respect to ATP concentration
were different, in that the 45-kDa polypeptide exhibited a
sigmoidal response while a rectangular response was observed
with the 41-kDa isoform. These observations suggest that the
additional domain at the C terminus of the 45-kDa isoform
modulates the ATP regulation of activity. Lysine 169, at the
putative ATP-binding site of the 41-kDa form of Rbu-P2
carboxylase activase, was changed to arginine, isoleucine, and
threonine by directed mutagenesis. These mutations abolished
Rbu-P2 carboxylase activase and ATPase activities, as well as
the capability of the protein to bind ATP. These results
confirm that lysine 169 is an essential residue.
76 NAL Call. No.: 448.3 J82
Expression of the Xanthomonas campestris pv. vesicatoria hrp
gene cluster, which determines pathogenicity and
hypersensitivity on pepper and tomato, is plant inducible.
Schulte, R.; Bonas, U.
Washington, D.C. : American Society for Microbiology; 1992
Feb. Journal of bacteriology v. 174 (3): p. 815-823; 1992 Feb.
Includes references.
Language: English
Descriptors: Xanthomonas campestris pv. vesicatoria; Genes;
Pathogenicity; Hypersensitivity; Capsicum annuum; Lycopersicon
esculentum; Gene expression; Nicotiana tabacum; Metabolites
Abstract: The hrp gene cluster from Xanthomonas campestris
pv. vesicatoria determines functions necessary not only for
pathogenicity on the host plants pepper and tomato but also
for the elicitation of the hypersensitive reaction on
resistant host and nonhost plants. Transcriptional orientation
and expression of the hrp loci were determined with hrp::Tn3-
gus fusions. In addition, expression of the hrp loci was
studied by RNA hybridization experiments. Expression of the
hrp genes was not detectable after growth of the bacteria in
complex medium or in minimal medium. However, high levels of
induction of hrp gene expression were measured during growth
of the bacteria in the plant. To search for a plant molecule
responsible for this induction, we examined a variety of
materials of plant origin for their ability to induce hrp gene
expression. Filtrates from plant suspension cultures induced
hrp genes to levels comparable to those induced in the plant.
The inducing molecule(s) was found to be heat stable and
hydrophilic and to have a molecular mass of less than 1,000
daltons.
77 NAL Call. No.: QR360.A1J6
Expression strategy of the potato virus X triple gene block.
Morozov, S.Yu; Miroshnichenko, N.A.; Solovyev, A.G.; Fedorkin,
O.N.; Zelenina, D.A.; Lukasheva, L.I.; Karasev, A.V.; Dolja,
V.V.; Atabekov, J.G. Reading : Society for General
Microbiology; 1991 Aug.
The Journal of general virology v. 72 (pt.8): p. 2039-2042;
1991 Aug. Includes references.
Language: English
Descriptors: Potato x potexvirus; Gene expression; Rna;
Translation
Abstract: The mode of expression of the overlapping genes of
the triple block positioned internally in potato virus X (PVX)
RNA was examined. The results of In vitro translation of
synthetic RNA transcripts and natural PVX-specific
methylmercuric hydroxide-denatured dsRNAs suggest that the 25K
protein is expressed as a single translation product of the
2.1 kb subgenomic (sg) RNA and that both the 12K and 8K
proteins are expressed from the same 1.4 kb sgRNA.
78 NAL Call. No.: 450 P693
Factors affecting gene expression of patatin and proteinase-
inhibitor-II gene families in detached potato leaves:
implications for their co-expression in developing tubers.
Pena-Cortes, H.; Liu, X.J.; Serrano, J.S.; Schmid, R.;
Willmitzer, L. Berlin : Springer-Verlag; 1992.
Planta v. 186 (4): p. 495-502; 1992. Includes references.
Language: English
Descriptors: Solanum tuberosum; Leaves; Tubers; Gene
expression; Genetic regulation; Protein synthesis; Plant
proteins; Proteinase inhibitors
Abstract: In whole intact potato (Solanum tuberosum L.)
plants, the gene families of class-I patatin and proteinase
inhibitor II (Pin 2) are constitutively expressed in the
tubers. However, they are also induced in detached potato
leaves in the presence of light. To further characterize this
light action, the detached leaves were subjected to
monochromatic light of different wavelengths and to darkness
in the presence of metabolites and inhibitors. Patatin genes
could be induced by the simultaneous application of sucrose
(sugars) and glutamine in darkness. Neither of these
metabolites was active when supplied alone. When
photosynthesis was blocked by 3-(3,4-Dichlorophenyl)-1,1-
dimethylurea (DCMU) in the light, patatin genes were not
expressed; however, the inhibition was overcome in the
presence of sucrose. This indicates that besides its role in
photosynthetic carbohydrate production, light may be essential
for the supply of amino acids (or reduced nitrogen). Unlike
patatin, Pin 2 genes were, to a small extent, also active in
darkness, and sucrose weakly enhanced this expression.
However, DCMU did not affect Pin 2 expression in the light.
Both abscisic acid and methyl jasmonate strongly promoted the
accumulation of Pin 2 mRNA independent of the light
conditions, indicating that the gene family is probably under
hormonal control. The phytohormones did not affect patatin
gene expression. Inhibitors of cytosolic (cycloheximide) and
organellar (chloramphenicol) translation had opposite effects
on the two gene families. Careful evaluation of the
inhibitors' action indicates that protein synthesis (cytosol)
is required for the expression of Pin 2 genes but not for the
patatin genes. These results clearly demonstrate that,
although in situ both gene families are constitutively
expressed in the same plant organ (tuber) in intact plants,
their expression is mediated by different factors.
79 NAL Call. No.: SB732.6.M65
Fungal- and plant-specific gene markers to follow the bean
anthracnose infection process and normalize a bean chitinase
mRNA induction. Mahe, A.; Grisvard, J.; Dron, M.
St. Paul, Minn. : APS Press; 1992 May.
Molecular plant-microbe interactions : MPMI v. 5 (3): p.
242-248; 1992 May. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Colletotrichum
lindemuthianum; Host parasite relationships; Aspergillus
nidulans; Actin; Genes; Gene expression; Infection; Leaves;
Defense mechanisms; Chitinase; Enzyme activity; Messenger
RNA; Detection; Genetic markers; Quantitative techniques
80 NAL Call. No.: TP248.27.P55P52
Gene activity during tuber formation in the potato (Solanum
tuberosum). Bevan, M.
New York, N.Y. : Chapman and Hall; 1991.
Plant biotechnology v. 2: p. 75-93; 1991. In the series
analytic: Developmental regulation of plant gene expression /
edited by D. Grierson. Literature review. Includes
references.
Language: English
Descriptors: Solanum tuberosum; Genes; Gene expression;
Genetic regulation; Plant development; Tubers; Transgenics;
Genetic transformation; Literature reviews
81 NAL Call. No.: QK710.P62
Genes encoding the small subunit of ribulose 1,5-bisphosphate
carboxylase/oxygenase in Phaseolus vulgaris L.: nucleotide
sequence of cDNA clones and initial studies of expression.
Knight, M.R.; Jenkins, G.I.
Dordrecht : Kluwer Academic Publishers; 1992 Feb.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(3): p. 567-579; 1992 Feb. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Multigene families; Ribulose-
bisphosphate carboxylase; Nucleotide sequences; Amino acid
sequences; Introns; Gene expression; Messenger RNA; Leaves;
Genetic regulation; Light
Abstract: The small subunit of ribulose 1,5-bisphosphate
carboxylase/oxygenase (EC 4.1.1.39) in the French bean
Phaseolus vulgaris L. is encoded by a small gene family
consisting of a minimum of three members. Three small subunit
genes (rbcS genes) represented in a light-grown primary leaf
cDNA library were characterised by sequencing two cDNAs which
were full-length and one which was deficient in part of the
sequence encoding the transit peptide. The cDNA clones are
identical in their coding sequences, for both the transit
peptide and the mature polypeptide, but divergent in their
untranslated sequences. The derived amino acid sequence is
very similar to that reported for other species, although the
first amino acid of the mature polypeptide is isoleucine,
which differs from the methionine found in all other higher
plant rbcS genes. Surprisingly, one of the cDNA clones
contains two introns, which are at positions conserved in rbcS
genes from other species. It is concluded that this cDNA
resulted from the cloning of an unprocessed transcript.
Alternative polyadenylation sites are found for two of the
genes. Expression of the rbcS genes in the primary leaves is
stimulated by light, although transcripts can readily be
detected in dark-grown leaves. Expression is also organ-
specific, as in other species. The frequency of cDNA clones in
the library indicates that the different genes show
quantitative differences in expression and S1 nuclease
analysis suggests that individual rbcS genes are
photoregulated.
82 NAL Call. No.: aS21.R44A7
Genetic organization and expression of the tomato spotted wilt
virus genome. Haan, P. de; Kormelink, R.; Peters, D.;
Goldbach, R.
Beltsville, Md. : The Service; 1991 Feb.
ARS - U.S. Department of Agriculture, Agricultural Research
Service (87): p. 60-66; 1991 Feb. Paper presented at the USDA
Workshop "Virus-Thrips-Plant Interactions of Tomato Spotted
Wilt Virus," April 18-19, 1990, Beltsville, Maryland.
Includes references.
Language: English
Descriptors: Tomato spotted wilt virus; Gene expression;
Molecular genetics; Genome analysis
83 NAL Call. No.: QK725.P54
Genetic transformation of sweet potato by particle
bombardment. Prakash, C.S.; Varadarajan, U.
Berlin, W. Ger. : Springer International; 1992.
Plant cell reports v. 11 (2): p. 53-57; 1992. Includes
references.
Language: English
Descriptors: Ipomoea batatas; Genetic transformation; Gene
transfer; Gene expression; Genotypes; Chimeras; Marker genes;
Transgenics; Callus; Roots; Regenerative ability
Abstract: Transient and stable expression of foreign genes
has been achieved in sweet potato using the particle
bombardment system of gene delivery. Callus and root isolates
of two genotypes (Jewel and TIS-70357) with positive signs of
transformation have been recovered. Tungsten microcarriers
coated with plasmid DNA (pBI 221 containing the gusA gene)
were accelerated at high velocity using a biolistic device
into sweet potato target tissues. Histochemical examination of
bombarded leaf and petiole explants revealed that most had
cells expressing the gusA gene. When explants were cultured,
calli and roots developed in most bombarded tissues. Similar
results but with a lower frequency of transformation were
observed when the plasmid pBI 121 (with gusA and antibiotic
resistance npt II genes) was employed and bombarded explants
cultured on an antibiotic selection medium. Subcultured roots
and calli were positive for gusA expression when tested even
after one year of in vitro culture, and thus the expression of
the foreign gene is fairly stable. The particle bombardment
approach of gene delivery appears to have a potential for
generating transgenic sweet potatoes with useful agronomic
traits.
84 NAL Call. No.: SB732.6.M65
Genetically engineered resistance to potato virus S in potato
cultivar Russet Burbank.
MacKenzie, D.J.; Tremaine, J.H.; McPherson, J.
St. Paul, Minn. : APS Press; 1991 Jan.
Molecular plant-microbe interactions : MPMI v. 4 (1): p.
95-102; 1991 Jan. Includes references.
Language: English
Descriptors: Solanum tuberosum; Disease resistance; Potato s
carlavirus; Genetic resistance; Gene transfer; Coat proteins;
Genes; Genetic transformation; Agrobacterium tumefaciens;
Regeneration; Transgenics; Gene expression; Induced
resistance; Potato m carlavirus; Potato x potexvirus; Host
parasite relationships
85 NAL Call. No.: QH426.C8
Genomic organization and sequence analysis of the cytochrome
oxidase subunit II gene from normal and male-sterile
mitochondria in sugar beet. Senda, M.; Harada, T.; Mikami, T.;
Sugiura, M.; Kinoshita, T. Berlin, W. Ger. : Springer
International; 1991.
Current genetics v. 19 (3): p. 175-181; 1991. Includes
references.
Language: English
Descriptors: Beta vulgaris; Mitochondrial genetics;
Cytoplasmic male sterility; Cytochrome-c oxidase; Multiple
genes; Nucleotide sequences; Restriction mapping; Introns;
Amino acid sequences; Gene mapping; Mitochondrial DNA;
Recombination; Gene expression; Messenger RNA
Abstract: We have cloned and sequenced the cytochrome oxidase
subunit II (coxII) gene from both normal and cytoplasmic male-
sterile (CMS) sugar beet. The normal coxII (designated NcoxII)
locus was found to be located 1491 bp upstream from the gene
for cytochrome oxidase subunit I (coxI) on the same DNA strand
and to have a 1463 bp intron which split the coding sequence
into two exons (382 and 398 bp). The COXII protein contains
260 amino acid residues. We have also found two copies of the
coxII gene (ScoxII-1 and ScoxII-2) to be present in the CMS
genome. Our results suggest that the NcoxII gene diverges
completely from the ScoxII-1 and ScoxII-2 genes 50 bp 5' to
the ATG start codon. In addition, the ScoxII-1 and ScoxII-2
sequences could be readily discriminated from each other by
the 3' end and the immediately adjacent flanking sequences of
the gene: the 3' divergence results in a 101 codon extension
of the ScoxII-2 ORF. Northern blot analysis demonstrates that
the coxII gene exhibits altered transcript patterns in CMS
compared with normal sugar beet. Different genomic
arrangements of the coxII gene are considered to be the result
of extensive intra- and inter-molecular recombination events
involving the repeated DNA elements in the mitochondrial
genome.
86 NAL Call. No.: QK710.P62
The glucosinolate-degrading enzyme myrosinase in Brassicaceae
is encoded by a gene family.
Xue, J.; Lenman, M.; Falk, A.; Rask, L.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 387-398; 1992 Jan. Includes references.
Language: English
Descriptors: Sinapis alba; Brassica napus; Arabidopsis
thaliana; Multigene families; Thioglucosidase; Nucleotide
sequences; Gene expression; Messenger RNA; Amino acid
sequences
Abstract: A full-length cDNA clone (MB3) and three partial
clones (MA1, MB1 and MB2) which encode myrosinase
(thioglucoside glucohydrolase, EC 3.2.3.1) were isolated from
a Sinapis alba (white mustard) cDNA library. Nucleotide
sequence analysis of these clones revealed that they are
encoded by a gene family. Southern blot analysis with gene-
specific probes showed that the gene family consists of a
least two subfamilies (MA and MB) each with several members
both in S. alba and in Brassica napus (oilseed rape). In
Arabidopsis thaliana (wall cress) only three myrosinase genes
seem to be present. Northern blot analysis indicated that all
the myrosinase mRNA species have the same size, approximately
1.95 kb.
87 NAL Call. No.: 442.8 Z34
Glyphosate selected amplification of the 5-
enolpyruvylshikimate-3-phosphate synthase gene in cultured
carrot cells.
Shyr, Y.Y.J.; Hepburn, A.G.; Widholm, J.M.
Berlin, W. Ger. : Springer International; 1992 Apr.
M G G : Molecular and general genetics v. 232 (3): p. 377-382;
1992 Apr. Includes references.
Language: English
Descriptors: Daucus carota; Structural genes; Transferases; In
vitro selection; Glyphosate; Herbicide resistance;
Amplification; Gene expression; Messenger RNA; Gene dosage;
Tissue culture; Cell suspensions
Abstract: CAR and C1, two carrot (Dacus carota L.) suspension
cultures of different genotypes, were subjected to stepwise
selection for tolerance to the herbicide glyphosate [(N-
phosphonomethyl)glycine]. The specific activity of the target
enzyme, 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS),
as well as the mRNA level and copy number of the structural
gene increased with each glyphosate selection step. Therefore,
the tolerance to glyphosate is due to stepwise amplification
of the EPSPS genes. During the amplification process, DNA
rearrangement did not occur within the EPSPS gene of the CAR
cell line but did occur during the selection step from 28 to
35 mM glyphosate for the C1 cell line, as determined by
Southern hybridization of selected cell DNA following EcoRI
restriction endonuclease digestion. Two cell lines derived
from a previously selected glyphosate-tolerant cell line (PR),
which also had undergone EPSPS gene amplification but have
been maintained in glyphosate-free medium for 2 and 5 years,
have lost 36 and 100% of the increased EPSPS activity,
respectively. Southern blot analysis of these lines confirms
that the amplified DNA is relatively stable in the absence of
selection. These studies demonstrate that stepwise selection
for glyphosate resistance reproducibly produces stepwise
amplification of the EPSPS genes. The relative stability of
this amplification indicates that the amplified genes are not
extrachromosomal.
88 NAL Call. No.: QK725.P532
Heat shock gene expression is controlled primarily at the
translational level in carrot cells and somatic embryos.
Apuya, N.R.; Zimmerman, J.L.
Rockville, Md. : American Society of Plant Physiologists; 1992
Jun. The Plant cell v. 4 (6): p. 657-665; 1992 Jun. Includes
references.
Language: English
Descriptors: Daucus carota; Gene expression; Translation;
Multigene families; Heat shock proteins; Callus; Somatic
embryogenesis; Heat shock; Genetic regulation; Messenger RNA;
Plant embryos; Ribosomes
Abstract: We have determined that the synthesis of heat shock
proteins is regulated ultimately at the translational level in
heat-shocked carrot callus cells and somatic embryos. Polysome
analysis revealed that heat-shocked callus cells do not
translate most heat shock transcripts, which they abundantly
synthesize and accumulate. By contrast, heat-shocked globular
embryos accumulate low levels of heat shock mRNA but
selectively translate more of the heat shock mRNA molecules
compared to callus cells and embryos of later stages. The
overall result of these different translational control
schemes is that undifferentiated callus cells and globular
embryos synthesize comparable levels of heat shock proteins
even though they have large differences in heat shock
transcript levels.
89 NAL Call. No.: QK710.P68
Identification of a cDNA for the plastid-located
geranylgeranyl pyrophosphate synthase from Capsicum annuum:
correlative increase in enzyme activity and transcript level
during fruit ripening.
Kuntz, M.; Romer, S.; Suire, C.; Hugueney, P.; Weil, J.H.;
Schantz, R.; Camara, B.
Oxford : Blackwell Scientific Publishers and BIOS Scientific
Publishers; 1992 Jan.
The plant journal v. 2 (1): p. 25-34; 1992 Jan. Includes
references.
Language: English
Descriptors: Capsicum annuum; Fruit; Chemical composition;
Pyrophosphates; Ligases; Purification; Enzyme activity;
Ripening; Transcription; Genetic code; Cloning; Gene
expression; Terpenoids; Biosynthesis; Nucleotide sequences;
Amino acid sequences
90 NAL Call. No.: 500 N21P
Identification of a tomato gene for the ethylene-forming
enzyme by expression in yeast.
Hamilton, A.J.; Bouzayen, M.; Grierson, D.
Washington, D.C. : The Academy; 1991 Aug15.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (16): p. 7434-7437; 1991 Aug15.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Saccharomyces
cerevisiae; Amino acid sequences; Biosynthesis; Ethylene;
Enzyme activity; Gene expression; Genetic transformation;
Molecular genetics; Nucleotide sequences; Oxidoreductases
Abstract: The ethylene-forming enzyme (EFE), which catalyzes
the last step in the biosynthesis of the plant hormone
ethylene, has never been purified and no molecular probes are
available. Recently, a putative cDNA done for tomato EFE
(pTOM13) has been identified by inhibiting ethylene synthesis
with an antisense gene expressed in transgenic plants. A
direct test of its function has been made by expression of a
pTOM13 gene in Saccharomyces cerevisiae. After cloning
artefacts were discovered in the 5' region of the cDNA, a
corrected cDNA (pRC13) was created by the fusion of the 5' end
of a genomic clone to the 3' end of the cDNA and expressed in
S. cerevisiae. Cultures of transformed yeast converted 1-
aminocyclopropane-l-carboxylic acid (ACC) to ethylene, whereas
control cells did not. This EFE activity displays similar
characteristics to EFE found in plant tissue: it converts the
trans isomer of the ACC analogue 1-amino-2-ethylcyclopropane-
l-carboxylic acid to 1-butene in preference to the cis isomer,
and it is strongly inhibited by cobaltous ions and 1,10-
phenanthroline. Furthermore, information gained from the
activity of effectors on yeast EFE activity supports the
hypothesis that EFE is one of a group of hydroxylase enzymes.
91 NAL Call. No.: QK710.P62
An in planta induced gene of Phytophthora infestans codes for
ubiquitin. Pieterse, C.M.J.; Risseeuw, E.P.; Davidse, L.C.
Dordrecht : Kluwer Academic Publishers; 1991 Oct.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(4): p. 799-811; 1991 Oct. Includes references.
Language: English
Descriptors: Phytophthora infestans; Multigene families; Plant
proteins; Nucleotide sequences; Amino acid sequences; Gene
expression; Blight; Solanum tuberosum
Abstract: An in planta induced gene of Phytophthora infestans
(the causal organism of potato late blight) was selected from
a genomic library by differential hybridization using labelled
cDNA derived from poly(A)+ RNA of P. infestans grown in vitro
and labelled cDNA made from potato-P. infestans interaction
poly(A)+ RNA as probes. Sequence analysis showed that the gene
codes for ubiquitin, a highly conserved protein which plays an
important role in several cellular processes. The structure of
the polyubiquitin gene (designated ubi3R) is consistent with
the structure of other known polyubiquitin genes. It consists
of three repeats in a head-to-tail arrangement without
intervening sequences, each encoding a ubiquitin unit of 76
amino acids. The last ubiquitin unit is followed by an extra
asparagine residue at the carboxy-terminal end. Northern and
Southern blot analyses revealed that the polyubiquitin gene is
a member of a multigene family, all genes of which show
induced expression in planta.
92 NAL Call. No.: SB732.6.M65
In situ localization of Rhizobium mRNAs in pea root nodules:
nifA and nifH localization.
Yang, W.C.; Horvath, B.; Hontelez, J.; Kammen, A. van;
Bisseling, T. St. Paul, Minn. : APS Press; 1991 Sep.
Molecular plant-microbe interactions : MPMI v. 4 (5): p.
464-468; 1991 Sep. Includes references.
Language: English
Descriptors: Pisum sativum; Root nodules; Detection; Messenger
RNA; Nitrogen fixation; Genes; Rhizobium leguminosarum;
Biotypes; Strains; Gene expression; Nodulins; Nitrogenase
93 NAL Call. No.: 500 N21P
In vitro assembly of apophytochrome and apophytochrome
deletion mutants expressed in yeast with phycocyanobilin.
Deforce, L.; Tomizawa, K.I.; Ito, N.; Farrens, D.; Song, P.S.;
Furuya, M. Washington, D.C. : The Academy; 1991 Dec01.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (23): p. 10392-10396. ill; 1991 Dec01.
Includes references.
Language: English
Descriptors: Saccharomyces cerevisiae; Yeasts; Mutants;
Recombination; Gene expression; Phytochrome; Biosynthesis;
Amino acid sequences
Abstract: Recombinant pea type I phytochrome apoprotein
expressed in yeast is shown to assemble in vitro with
phycocyanobilin to produce a photoreversible phytochrome-like
adduct. As an initial investigation of the amino acid sequence
requirements for chromophore incorporation, three phyA gene
product deletion mutants were produced in yeast. Truncation of
the N-terminal tail to residue 46 demonstrates that this
region is not critical to bilin attachment, but a deletion
mutant lacking 222 amino acids from the N terminus failed to
yield holophytochrome in vitro, under the same conditions. A
mutant comprising a deletion of the C terminus to residue 548
showed bilin incorporation and red/far-red photoreversibility,
indicating that bilin-apophytochrome assembly still occurred
even when the entire C-terminal domain was truncated.
94 NAL Call. No.: QD341.A2N8
In vivo analysis of plant pre-mRNA splicing using an
autonomously replicating vector.
McCullough, A.J.; Lou, H.; Schuler, M.A.
Oxford : IRL Press; 1991 Jun11.
Nucleic acids research v. 19 (11): p. 3001-3009; 1991 Jun11.
Includes references.
Language: English
Descriptors: Agrobacterium tumefaciens; Nicotiana; Cloning;
Polymerase chain reaction; Pisum sativum; Triticum aestivum;
Glycine max; Gene expression
Abstract: In this paper, we demonstrate that an autonomously
replicating plant expression vector can be used for analysis
of pre-mRNA splicing determinants in intact dicot cells. This
vector system relies on the Agrobacterium-mediated
transfection of leaf discs with the A component of the
geminivirus tomato golden mosaic virus (TGMV). Insertion of
intron sequences between viral promoter and terminator
sequences results in the production of high levels of pre-mRNA
transcripts that are effectively and accurately spliced in
vivo. Introns from the soybean B-conglycinin gene are spliced
at > 95% efficiency indicating that the high expression levels
of precursor RNA do not exceed the intron splicing capacity of
these cells. Introns from the pea and wheat rbcS genes are
spliced at 85% and 73% efficiency, respectively, indicating
that tobacco leaf disc nuclei are capable of effectively and
accurately processing particular dicot and monocot introns.
Inclusion of a dicot intron in an engineered construct results
in a five-fold enhancement of the level of mRNA stably
expressed in dicot nuclei.
95 NAL Call. No.: QH506.E46
In vivo import of a normal or mutagenized heterologous
transfer RNA into the mitochondria of transgenic plants:
towards novel ways of influencing mitochondrial gene
expression?.
Small, I.; Marechal-Drouard, L.; Masson, J.; Pelletier, G.;
Cosset, A.; Weil, J.H.; Dietrich, A.
Oxford, Eng. : IRL Press; 1992 Apr.
The EMBO journal - European Molecular Biology Organization v.
11 (4): p. 1291-1296; 1992 Apr. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Solanum tuberosum;
Mitochondrial genetics; Transgenics; Genetic transformation;
Leucine; Transfer RNA; Genes; Uptake; Mitochondria; Gene
expression; Mutations; Gene transfer; Nucleotide sequences;
Molecular conformation
Abstract: Evidence that nuclear-encoded RNAs are present
inside mitochondria has been reported from a wide variety of
organisms, and is presumed to be due to import of specific
cytosolic RNAs. In plants, the first examples were the
mitochondrial leucine transfer RNAs of bean. In all cases, the
evidence is circumstantial, based on hybridization of the
mitochondrial RNAs to nuclear and not mitochondrial DNA. Here
we show that transgenic potato plants carrying a leucine tRNA
gene from bean nuclear DNA contain RNA transcribed from the
introduced gene both in the cytosol and inside mitochondria,
providing proof that the mitochondrial leucine tRNA is derived
from a nuclear gene and imported into the mitochondria. The
same bean gene carrying a 4 bp insertion in the anticodon loop
was also expressed in transgenic potato plants and the
transcript found to be present inside mitochondria, suggesting
that this natural RNA import system could eventually be used
to introduce foreign RNA sequences into mitochondria.
96 NAL Call. No.: SB732.6.M65
Incompatible interactions between crucifers and Xanthomonas
campestris involve a vascular hypersensitive response: role of
the hrpX locus. Kamoun, S.; Kamdar, H.V.; Tola, E.; Kado, C.I.
St. Paul, Minn. : APS Press; 1992 Jan.
Molecular plant-microbe interactions : MPMI v. 5 (1): p.
22-33; 1992 Jan. Includes references.
Language: English
Descriptors: Brassica campestris; Brassica juncea; Brassica
oleracea; Raphanus sativus; Capsicum frutescens; Datura
stramonium; Xanthomonas campestris pv. campestris; Xanthomonas
campestris pv. armoraciae; Strains; Host specificity;
Pathogenicity; Genes; Mutagenesis; Loci; Mutants; Gene
expression; Incompatibility; Defense mechanisms; Stress
response; Suppression; Strain differences; Histochemistry
97 NAL Call. No.: QH442.B5
Increased resistance to potato virus X and preservation of
cultivar properties in transgenic potato under field
conditions.
Jongedijk, E.; Schutter, A.A.J.M. de; Stolte, T.; Elzen,
P.J.M. van den; Cornelissen, B.J.C.
New York, N.Y. : Nature Publishing Company; 1992 Apr.
Bio/technology v. 10 (4): p. 422-429; 1992 Apr. Includes
references.
Language: English
Descriptors: Solanum tuberosum; Potato x potexvirus; Genetic
resistance; Transgenics; Genetic transformation; Coat
proteins; Genes; Gene expression; Cultivars; Agronomic
characteristics; Genetic engineering
98 NAL Call. No.: 450 P692
Induction of 1-aminocyclopropane-1-carboxylate synthase mRNA
by auxin in mung bean hypocotyls and cultured apple shoots.
Kim, W.T.; Silverstone, A.; Yip, W.K.; Dong, J.G.; Yang, S.F.
Rockville, Md. : American Society of Plant Physiologists; 1992
Feb. Plant physiology v. 98 (2): p. 465-471; 1992 Feb.
Includes references.
Language: English
Descriptors: Vigna radiata; Malus sylvestris; Shoots;
Hypocotyls; Genetic analysis; Rna; Dna amplification; Acc;
Ligases; Enzyme activity; Auxins; Gene expression; Ethylene
production; Transcription; Genetic code; Nucleotide sequences;
Amino acid sequences
Abstract: Auxin is known to promote ethylene production in
vegetative tissues by increasing the activity of 1-
aminocyclopropane-l-carboxylate (ACC) synthase; therefore, we
have studied the effect of auxins on ACC synthase mRNA
expression. Total RNA was isolated from auxin-incubated
cultured apple (Malus sylvestris Mill.) shoots or mung bean
(Vigna radiata L.) hypocotyls. These RNAs and a set of
oligonucleotide primers corresponding to two conserved amino
acid sequences (SNPLGTT and MSSFGLV) found in ACC synthases
isolated from other species were used for polymerase chain
reaction-based amplification of DNA fragments encoding the ACC
synthase-active site domain. We obtained and sequenced a 290-
base pair cDNA fragment (pAA1) from cultured apple shoots and
a 328-base pair cDNA clone (pMBA1) from mung bean hypocotyls.
Comparisons of their deduced amino acid sequences with those
of previously characterized ACC synthase cDNAs indicate that
both fragments are, indeed, closely related to ACC synthase
cDNA. Northern blot analyses further showed that the
expression of these transcripts is regulated by auxin
treatment. These data indicate that auxin induces ethylene
production transcriptionally by increasing the ACC synthase
transcripts. The pAA1 shares 46% amino acid sequence homology
with ripening-regulated apple fruit ACC synthase, indicating
that ripening-regulated and auxin-regulated ACC synthases are
encoded by different genes. In mung bean hypocotyls,
aminooxyacetic acid, a potent inhibitor of ACC synthase
activity, promoted the expression of auxin-induced ACC
synthase mRNA, but cycloheximide inhibited this induction.
99 NAL Call. No.: QK725.P532
Induction of malate synthase gene expression in senescent and
detached organs of cucumber.
Graham, I.A.; Leaver, C.J.; Smith, S.M.
Rockville, Md. : American Society of Plant Physiologists; 1992
Mar. The Plant cell v. 4 (3): p. 349-357; 1992 Mar. Includes
references.
Language: English
Descriptors: Cucumis sativus; Nicotiana plumbaginifolia;
Genes; Ligases; Gene expression; Genetic regulation;
Cotyledons; Senescence; Messenger RNA; Transcription; Beta-
glucuronidase; Reporter genes; Leaves; Corolla
Abstract: Expression of the malate synthase (MS) gene is
activated in cotyledons of cucumber seedlings during
postgerminative growth and then repressed as the cotyledons
become photosynthetic. MS gene expression is subsequently
reactivated in the cotyledons as they senesce a few weeks
later. In situ hybridization revealed that MS RNA is
distributed throughout the organ during postgerminative growth
and senescence, showing that the same cells express the gene
at different stages of development. MS RNA also appears in
senescing leaves and petals of cucumber plants. In addition,
we found that MS RNA appears in mature expanded leaves and
roots when they are removed from the plant and incubated in
darkness for several days, thus providing a potential
experimental system for the manipulation of MS gene
expression. Leaves from transgenic Nicotiana plumbaginifolia
containing the cucumber MS promoter fused to the beta-
glucuronidase (GUS) reporter gene accumulated GUS activity
when detached, demonstrating an activation of transcription
from the MS promoter following leaf excision. These results
are discussed in terms of the metabolic regulation of MS gene
expression.
100 NAL Call. No.: 81 SO12
Inheritance of viral bean leaf roll tolerance in peas.
Baggett, J.R.; Hampton, R.O.
Alexandria, Va. : The Society; 1991 Jul.
Journal of the American Society for Horticultural Science v.
116 (4): p. 728-731; 1991 Jul. Includes references.
Language: English
Descriptors: Idaho; Pisum sativum; Inheritance; Tolerance;
Bean leaf roll luteovirus; Crosses; Screening; Gene
expression; Major genes; Recessive genes
Abstract: The inheritance of tolerance to infection by bean
leaf roll luteovirus (BLRV) in Pisum sativum L. was studied in
the cross of cv. Parlay (sensitive to BLRV infection) X cv.
Oregon Sugarpod II (BLRV tolerant). The parents, reciprocal
F1, back-crosses, F2, and 234 random F3 families were screened
in 1986 and 1987 in the field at Twin Falls, Idaho, under
natural BLRV inoculation by aphids. Overall disease index
scores for the F1, F2, and F3 were about intermediate between
indices of the parents, with the F1 usually slightly higher
than midparent values. Backcross disease indices were
intermediate between the F1 and the respective parent
involved. Distribution of individual F3 family indices was
continuous and semi-normal. BLRV-sensitivity ranges within
parents and selected cultivars, as well as segregating
populations showed continuous variation and differed between
the 2 years, suggesting that expression of a major gene was
significantly influenced by natural variation in BLRV
inoculation pressure and timing. An apparent "additive gene
action" was probably an artifact of nonuniform timing and
levels of infection within plant populations. Chi-square
analyses of segregating populations indicated that a major
recessive gene, called lrv, conferred BLR disease tolerance.
101 NAL Call. No.: 450 P692
Inhibition of sucrose enhancer effect of the potato proteinase
inhibitor II promoter by salicylic acid.
Kim, S.R.; Kim, Y.; Costa, M.A.; An, G.
Rockville, Md. : American Society of Plant Physiologists; 1992
Apr. Plant physiology v. 98 (4): p. 1479-1483; 1992 Apr.
Includes references.
Language: English
Descriptors: Nicotiana tabacum; Transgenics; Gene expression;
Salicylic acid; Proteinase inhibitors; Promoters; Sucrose;
Enzyme activity
Abstract: Effect of salicylic acid (SA) on the expression of
the potato proteinase inhibitor (PI) II promoter was studied
with transgenic tobacco plants (Nicotiana tabacum) carrying a
gene fusion between the PI-II promoter and the chloramphenicol
acetyltransferase (cat) reporter. As previously observed, the
PI-II promoter was inducible by wounding and the promoter
activity was further enhanced by sucrose. Addition of SA did
not influence the wound induction of the PI-II promoter but
significantly inhibited the sucrose response. The 5'-deletion
mutant -573 was unable to respond to wounding but did respond
to sucrose and SA. The 3'-deletion analysis indicated the
presence of a sucrose-responsive element between -574 and
-520. A study of the insertion mutants revealed the function
of another sucrose-responsive element between -522 and -500.
Enhancer effects of these sucrose-responsive elements were
inhibited by SA. These studies suggest that SA inhibits PI-II
promoter activity by decreasing the sucrose response. Analysis
of SA-related chemicals revealed that only acetyl-SA showed a
similar inhibitory effect, and other hydroxybenzoic acids had
little or no effect on the sucrose enhancer activity.
Therefore, it seems that the interaction between SA and the
receptor molecule is specific.
102 NAL Call. No.: QH506.E46
Inhibition of the ADP-glucose pyrophosphorylase in transgenic
potatoes leads to sugar-storing tubers and influences tuber
formation and expression of tuber storage protein genes.
Muller-Rober, B.; Sonnewald, U.; Willmitzer, L.
Oxford, Eng. : IRL Press; 1992 Apr.
The EMBO journal - European Molecular Biology Organization v.
11 (4): p. 1229-1238; 1992 Apr. Includes references.
Language: English
Descriptors: Solanum tuberosum; Genetic transformation;
Transgenics; Nucleotidyltransferases; Structural genes;
Chimeras; Antisense RNA; Enzyme activity; Starch; Glucose;
Sucrose; Carbohydrate metabolism; Tubers; Plant development;
Dry matter accumulation; Plant proteins; Messenger RNA;
Hexosyltransferases; Gene expression
Abstract: Transgenic potato plants were created in which the
expression of ADP-glucose pyrophosphorylase (AGPase) was
inhibited by introducing a chimeric gene containing the coding
region of one of the subunits of the AGPase linked in an
antisense orientation to the CaMV 35S promoter. Partial
inhibition of the AGPase enzyme was achieved in leaves and
almost complete inhibition in tubers. This resulted in the
abolition of starch formation in tubers, thus proving that
AGPase has a unique role in starch biosynthesis in plants.
Instead up to 30% of the dry weight of the transgenic potato
tubers was represented by sucrose and up to 8% by glucose. The
process of tuber formation also changed, resulting in
significantly more tubers both per plant and per stolon. The
accumulation of soluble sugars in tubers of antisense plants
resulted in a significant increase of the total tuber fresh
weight, but a decrease in dry weight of tubers. There was no
significant change in the RNA levels of several other starch
biosynthetic enzymes, but there was a great increase in the
RNA level of the major sucrose synthesizing enzyme sucrose
phosphate synthase. In addition, the inhibition of starch
biosynthesis was accompanied by a massive reduction in the
expression of the major storage protein species of potato
tubers, supporting the idea that the expression of storage
protein genes is in some way connected to carbohydrate
formation in sink storage tissues.
103 NAL Call. No.: QK725.P54
Introduction and differential use of various promoters in
pollen grains of Nicotiana glutinosa and Lilium longiflorum.
Leede-Plegt, L.M. van der; Ven, B.C.E. van de; Bino, R.J.;
Salm, T.P.M. van der; Tunen, A.J. van
Berlin, W. Ger. : Springer International; 1992.
Plant cell reports v. 11 (1): p. 20-24; 1992. Includes
references.
Language: English
Descriptors: Nicotiana; Lilium longiflorum; Genetic
transformation; Pollen; Vectors; Gene transfer; Chimeras;
Reporter genes; Beta-glucuronidase; Gene expression; Enzyme
activity
Abstract: As part of our research to develop an alternative
system for the transformation of recalcitrant plant species we
investigated the use of the male gametophyte as a
transformation vector. Therefore the activity of four
different promoters (CaMV 35S, LAT52, chiA PA2 and TR2') was
analyzed in pollen of a dicot (Nicotiana glutinosa) and a
monocot (Lilium longiflorum) plant species. Gene constructs in
which the beta-glucuronidase (GUS) gene was placed under the
control of these promoters were introduced in pollen using a
particle delivery system. No activity of the Cauliflower
Mosaic Virus (CaMV) 35S promoter was detected in pollen of
both N. glutinosa and L. longiflorum. The promoter of the
tomato flower-specific LAT52 gene was highly active in N.
glutinosa pollen but remained silent in L. longiflorum pollen.
A similar expression pattern was observed for the pollen-
specific Chalcone Flavanone Isomerase chiA PA2 promoter
originally isolated from petunia. The TR2' mannopine synthase
promoter of Agrobacterium tumefaciens, however, was active in
pollen from Solanaceous species and also in pollen from the
monocot L. longiflorum. This suggests that the TR2' promoter
is active in vegetative and sporogenous tissues of dicot and
monocot plant species.
104 NAL Call. No.: 442.8 Z34
Isolation and characterization of a cDNA from Cuphea
lanceolata encoding a beta-ketoacyl-ACP reductase.
Klein, B.; Pawlowski, K.; Horicke-Grandpierre, C.; Schell, J.;
Topfer, R. Berlin, W. Ger. : Springer International; 1992 May.
M G G : Molecular and general genetics v. 233 (1/2): p.
122-128; 1992 May. Includes references.
Language: English
Descriptors: Cuphea; Dna; Multiple genes; Multigene families;
Alcohol oxidoreductases; Nucleotide sequences; Amino acid
sequences; Enzyme activity; Amino acids; Gene expression;
Roots; Leaves; Flowers; Seeds
Abstract: A cDNA encoding beta-ketoacyl-ACP reductase (EC
1.1.1.100), an integral part of the fatty acid synthase type
II, was cloned from Cuphea lanceolata. This cDNA of 1276 bp
codes for a polypeptide of 320 amino acids with 63 N-terminal
residues presumably representing a transit peptide and 257
residues corresponding to the mature protein of 27 kDa. The
encoded protein shows strong homology with the amino-terminal
sequence and two tryptic peptides from avocado mesocarp beta-
ketoacyl-ACP reductase, and its total amino acid composition
is highly similar to those of the beta-ketoacyl-ACP reductases
of avocado and spinach. Amino acid sequence homologies to
polyketide synthase, beta-ketoreductases and short-chain
alcohol dehydrogenases are discussed. An engineered fusion
protein lacking most of the transit peptide, which was
produced in Escherichia coli, was isolated and proved to
possess beta-ketoacyl-ACP reductase activity. Hybridization
studies revealed that in C. lanceolata beta-ketoacyl-ACP
reductase is encoded by a small family of at least two genes
and that members of this family are expressed in roots,
leaves, flowers and seeds.
105 NAL Call. No.: QK710.P62
Isolation and characterization of a cDNA that encodes ECP31,
an embryogenic-cell protein from carrot.
Kiyosue, T.; Yamaguchi-Shinozaki, K.; Shinozaki, K.; Higashi,
K.; Satoh, S.; Kamada, H.; Harada, H.
Dordrecht : Kluwer Academic Publishers; 1992 May.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(2): p. 239-249; 1992 May. Includes references.
Language: English
Descriptors: Daucus carota; Genes; Dna; Plant proteins;
Nucleotide sequences; Amino acid sequences; Messenger RNA;
Gene expression; Somatic embryogenesis; Plant embryos;
Embryogenesis; Genetic regulation; Abscisic acid
Abstract: A full-length cDNA for ECP31, an embryogenic cell
protein from carrot (Daucus carota L.) with a Mr of 31000
(Kiyosue T, Satoh S, Kamada H, Harada H (1991) Plant Physiol
95: 1077-1083), was isolated from a cDNA library prepared from
embryogenic cells using PCR-amplified DNA as a probe. The
genomic Southern blot analysis revealed that there are two or
three genes for ECP31 in the carrot genome. The transcripts of
ECP31 accumulated in the peripheral regions of clusters of
embryogenic cells and disappeared in the course of somatic
embryogenesis that was induced by transfer of the embryogenic
cells to auxin-free media. The cDNA encodes a polypeptide of
256 amino acids, and the calculated molecular weight of this
polypeptide is 26111. The deduced amino acid sequence shows a
high degree (62.2%) of similarity to that of a protein that is
abundant during late embryogenesis of cotton (LEA D34; Baker
JC, Steele C, Dure III (1988) Plant Mol Biol 11: 227-291). The
mRNAs for ECP31 started to accumulate in zygotic embryos at a
late stage of embryogenesis but were undetectable in mature
embryos within 24 h after imbibition of seeds. In dry fruits
(seeds), the transcripts were detected only in zygotic embryos
by in situ hybridization. The level of ECP31 transcripts
increased after treatment with abscisic acid (ABA) in torpedo-
shaped somatic embryos but not in seven-day-old seedlings.
These results suggest that both embryo-specific factor(s) and
ABA are involved in the expression of the gene for ECP31.
106 NAL Call. No.: QK710.P62
Isolation and characterization of a cDNA-clone coding for
potato type A phytochrome.
Heyer, A.; Gatz, C.
Dordrecht : Kluwer Academic Publishers; 1992 Feb.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(3): p. 535-544; 1992 Feb. Includes references.
Language: English
Descriptors: Solanum tuberosum; Genes; Phytochrome; Nucleotide
sequences; Amino acid sequences; Gene expression; Messenger
RNA; Seedlings; Sprouts; Light; Etiolation; Leaves; Roots;
Dark
Abstract: We have isolated and sequenced a cDNA clone
encoding the apoprotein of a potato phytochrome. Based on the
deduced amino acid sequence, which shows 78% amino acid
identity to the Arabidopsis phyA and 50% identity to the
Arabidopsis phyB open reading frame, we have classified this
cDNA clone as potato phyA phytochrome. The amino acid
immediately preceding cysteine 323, which is the homologue of
oat cystein 321, to which the chromophore has been shown to be
attached, is a tyrosine residue. This contrasts with six other
type A phytochrome sequences from both monocots and dicots
that encode serine in this position. As already observed in
three other cDNAs isolated from dicot species, the potato phyA
clone encodes a short open reading frame (13 amino acids)
preceding the phyA open reading frame (1123 amino acids),
supporting the idea that this type of leader sequence might be
involved in the regulated expression of the phytochrome
apoprotein. Southern blot analysis revealed a single phyA gene
as well as other related phytochrome sequences in the potato
genome. phyA mRNA levels varied in different organs and were
modulated by white light; in seedlings and sprouts, highest
levels of mRNA were detected in the etiolated stage. Upon
illumination with white light, mRNA levels decreased to the
amount found in leaves of re-etiolated plants. Lowest
expression was observed in leaves of plants grown in the
light, in tubers irrespective of light treatment, and in roots
of plants grown in the dark. In roots of plants grown in the
light, elevated levels of phyA mRNA were detected. Using a
monoclonal antibody generated against pea phytochrome as an
immunochemical probe, the protein was only detectable in
protein extracts from etiolated seedlings and sprouts.
107 NAL Call. No.: QK710.P62
Isolation and characterization of a gene encoding a
chlorophyll a/b-binding protein from mustard and the targeting
of the encoded protein to the thylakoid membrane of pea
chloroplasts in vitro.
Gauly, A.; Batschauer, A.; Arnim, A. von; Kossel, H.
Dordrecht : Kluwer Academic Publishers; 1992 May.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(2): p. 277-287; 1992 May. Includes references.
Language: English
Descriptors: Sinapis alba; Pisum sativum; Multigene families;
Structural genes; Chlorophyll a/b binding protein; Nucleotide
sequences; Amino acid sequences; Transcription; Gene
expression; Translation; Protein transport; Thylakoids; Plasma
membranes; In vitro; Light harvesting complexes; Chloroplasts
Abstract: Three independent clones carrying a mustard gene
coding for the chlorophyll a/b-binding protein were isolated
by screening a genomic library of mustard with a heterologous
cDNA probe from pea. All of them encode the same CAB gene,
which, as shown by sequence analysis and comparison with
published CAB sequences, belongs to the family of type I PSII
CAB genes, encoding a precursor protein of 266 amino acids.
Several conserved sequence motifs are observed in the 5' and
3' non-coding region of the gene. The putative transcription
start site could be localized to 60 bp upstream of SA-CAB1
initiator codon by S1 mapping. Plasmids were constructed which
allow in vitro transcription and translation of the whole
chlorophyll a/b-binding protein and of truncated species which
lack increasing portions of the C-terminus. Whereas the in
vitro import into pea chloroplasts is not affected by these C-
terminal deletions, targeting to the thylakoid membrane is
abolished by the removal of the C-terminal helical domain.
Accordingly, the 54 amino acids which contain the C-terminal
membrane-spanning helix and flanking regions is an essential
component of the thylakoid targeting signal.
108 NAL Call. No.: 442.8 Z34
Isolation and characterization of nitrate reductase-deficient
mutants in tomato (Lycopersicon esculentum Mill.).
Schoenmakers, H.C.H.; Koornneef, M.; Alefs, S.J.H.M.; Gerrits,
W.F.M.; Kop, D. van der; Cherel, I.; Caboche, M.
Berlin, W. Ger. : Springer International; 1991 Jul.
M G G : Molecular and general genetics v. 227 (3): p. 458-464;
1991 Jul. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Induced mutations;
Mutants; Nitrate reductase; Enzyme deficiencies; Chlorates;
Resistance; Selection; Seedlings; Recessive genes;
Complementation; Segregation; Chlorosis; Nitrate; Leaves;
Coenzymes; Messenger RNA; Gene expression; Xanthine
dehydrogenase; Enzyme activity
Abstract: Five nitrate reductase-deficient mutants of tomato
were isolated from an M2 population after
ethylmethanesulphonate (EMS) seed treatment by means of
selection for chlorate resistance. All mutations were
monogenic and recessive and complementation analysis revealed
that they were non-allelic. Biochemical and molecular
characterization of these mutants showed that four of them are
cofactor mutants while one is an apoenzyme mutant.
109 NAL Call. No.: SB732.6.M65
Isolation and characterization of Rhizobium (IC3342) genes
that determine leaf curl induction in pigeon pea.
Upadhyaya, N.M.; Scott, K.F.; Tucker, W.T.; Watson, J.M.;
Dart, P.J. St. Paul, Minn. : APS Press; 1992 Mar.
Molecular plant-microbe interactions : MPMI v. 5 (2): p.
129-143; 1992 Mar. Includes references.
Language: English
Descriptors: Cajanus cajan; Rhizobium; Strains; Mutants; Plant
disorders; Leaves; Phenotypes; Genetic analysis; Nucleotide
sequences; Amino acid sequences; Gene expression; Genes; Dna;
Characterization; Comparisons; Rhizobium meliloti; Escherichia
coli
110 NAL Call. No.: QK710.P62
Isolation and characterization of tomato cDNA and genomic
clones encoding the ubiquitin gene ubi3.
Hoffman, N.E.; Ko, K.; Milkowski, D.; Pichersky, E.
Dordrecht : Kluwer Academic Publishers; 1991 Dec.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(6): p. 1189-1201; 1991 Dec. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Cloning; Plant
proteins; Promoters; Nucleotide sequences; Restriction
fragment length polymorphism; Gene location; Gene mapping;
Gene expression; Messenger RNA; Chloroplasts; Amino acid
sequences; Genetic regulation; Light; Heat shock
Abstract: We report here the isolation and nucleotide
sequence of tomato cDNA and genomic clones encoding a
ubiquitin extension protein homologous to the yeast gene ubi3.
Sites similar to upstream activating sites commonly found in
the promoters of yeast ribosomal genes were observed in the
tomato promoter. The tomato ubi3 promoter also contained
elements found in the rbcS promoter from pea. The
transcription initiation site was determined to occur 66 bp
upstream of the initiating Met. RFLP mapping revealed that the
gene was located on chromosome 1, 23 cM from marker TG301. A
ubi3 gene-specific probe hybridized to a single 800 nt
transcript. Expression was reduced in heat-shocked plants and
plants kept in the dark. Expression was highest in young
leaves and immature green fruit and lowest in mature leaves
and petals. We isolated the original cDNA clone using an
antibody prepared against chloroplast polypeptides.
Immunological studies did not detect ubiquitin or ubiquitin
extension proteins in the chloroplast. However, higher-
molecular-weight chloroplast proteins were detected with
ubiquitin antisera suggesting that ubiquitin conjugates are
transported into the chloroplast.
111 NAL Call. No.: QP501.E8
Isolation, characterization, and sequence analysis of a cDNA
clone encoding L-protein, the dihydrolipoamide dehydrogenase
component of the glycine cleavage system from pea-leaf
mitochondria.
Bourguignon, J.; Macherel, D.; Neuburger, M.; Douce, R.
New York, NY : Springer-Verlag New York Inc; 1992 Mar.
European journal of biochemistry v. 204 (2): p. 865-873; 1992
Mar. Includes references.
Language: English
Descriptors: Pisum sativum; Leaves; Mitochondria;
Photorespiration; Plant proteins; Glycine; Oxidoreductases;
Clones; Nucleotide sequences; Amino acid sequences; Isolation;
Characterization; Structure activity relationships; Gene
expression; Messenger RNA
Abstract: L-protein is the dihydrolipoamide dehydrogenase
component of the glycine decarboxylase complex which
catalyses, with serine hydroxymethyltransferase, the
mitochondrial step of photorespiration. We have isolated and
characterized a cDNA from a lambda gt11 pea library encoding
the complete L-protein precursor. The derived amino acid
sequence indicates that the protein precursor consists of 501
amino acid residues, including a presequence peptide of 31
amino acid residues. The N-terminal sequence of the first 18
amino acid residues of the purified L-protein confirms the
identity of the cDNA. Alignment of the deduced amino acid
sequence of L-protein with human, porcine and yeast
dihydrolipoamide dehydrogenase sequences reveals high
similarity (70% in each case), indicating that this enzyme is
highly conserved. Most of the residues located in or near the
active sites remain unchanged. The results described in the
present paper strongly suggest that, in higher plants, a
unique dihydrolipoamide dehydrogenase is a component of
different mitochondrial enzyme complexes. Confidence in this
conclusion comes from the following considerations. First,
after fractionation of a matrix extract of pea-leaf
mitochondria by gel-permeation chromatography followed by gel
electrophoresis and Western-blot analysis, it was shown that
polyclonal antibodies raised against the L-protein of the
glycine-cleavage system recognized proteins with an Mr of
about 60000 in different elution peaks where dihydrolipoamide
dehydrogenase activity has been detected. Second, Northern-
blot analysis of RNA from different tissues such as leaf,
stem, root and seed, using L-protein cDNA as a probe,
indicates that the mRNA of the dihydrolipoamide dehydrogenase
accumulates to high levels in all tissues. in contrast, the H-
protein (a specific protein component of the glycine-cleavage
system) is known to be expressed primarily in leaves. Third,
Southern-blot analysis indicated that the gene coding for L-
protein in p
112 NAL Call. No.: QH506.E46
Light-inducible and constitutively expressed DNA-binding
proteins recognizing a plant promoter element with functional
relevance in light responsiveness. Weisshaar, B.; Armstrong,
G.A.; Block, A.; Da Costa e Silva, O.; Hahlbrock, K. Oxford,
Eng. : IRL Press; 1991 Jul.
The EMBO journal - European Molecular Biology Organization v.
10 (7): p. 1777-1786; 1991 Jul. Includes references.
Language: English
Descriptors: Petroselinum crispum; Dna binding proteins;
Controlling elements; Binding site; Naringenin-chalcone
synthase; Promoters; Nucleotide sequences; Amino acid
sequences; Gene expression; Messenger RNA; Light; Genetic
regulation
Abstract: Four cis-acting elements, designated as Boxes I,
II, III and IV, have previously been identified as
functionally relevant components of the light-responsive
chalcone synthase (CHS) promoter in parsley (Petroselinum
crispum). This paper describes the isolation of three cDNAs
encoding proteins which bind specifically to Box II, one of
two cis-acting elements found within a 52 bp CHS promoter
region shown here to be sufficient for light responsiveness in
parsley. The deduced amino acid sequences of all three
proteins reveal conserved basic and leucine zipper domains
characteristic of transcription factors of the bZIP class.
Nucleotide sequences recognized by these factors contain an
ACGT motif common to many cis-acting elements. Therefore, we
have termed the proteins CPRF-1, -2 and -3 (Common Plant
Regulatory Factor). The characteristics of CPRF-1 binding to
Box II and the timing of transient CPRF-1 mRNA accumulation
during light exposure of previously dark-grown parsley cells
are consistent with the hypothesis that this factor
participates in the light-mediated activation of the CHS gene
in parsley.
113 NAL Call. No.: 442.8 Z34
Lipoxygenase gene expression is modulated in plants by water
deficit, wounding, and methyl jasmonate.
Bell, E.; Mullet, J.E.
Berlin, W. Ger. : Springer International; 1991 Dec01.
M G G : Molecular and general genetics v. 230 (3): p. 456-462;
1991 Dec01. Includes references.
Language: English
Descriptors: Glycine max; Genes; Lipoxygenase; Nucleotide
sequences; Amino acid sequences; Messenger RNA; Gene
expression; Genetic regulation; Water stress; Abiotic
injuries; Jasmonic acid; Leaves; Hypocotyls
Abstract: Two classes of lipoxygenase (LOX) cDNAs, designated
loxA and loxB, were isolated from soybean. A third
lipoxygenase cDNA, loxP1, was isolated from pea. The deduced
amino acid sequences of loxA and loxB show 61-74% identity
with those of soybean seed LOXs. loxA and loxB mRNAs are
abundant in roots and non-growing regions of seedling
hypocotyls. Lower levels of these mRNAs are found in hypocotyl
growing regions. Exposure of soybean seedlings to water
deficit causes a rapid increase in loxA and loxB mRNAs in the
elongating hypocotyl region. Similarly, loxP1 mRNA levels
increase rapidly when pea plants are wilted. loxA and loxB
mRNA levels also increase in wounded soybean leaves, and these
mRNAs accumulate in soybean suspension cultures treated with
20 micromole methyl jasmonate. These results demonstrate that
LOX gene expression is modulated in response to water deficit
and wounding and suggest a role for lipoxygenase in plant
responses to these stresses.
114 NAL Call. No.: QK710.P68
The MADS box gene family in tomato: temporal expression during
floral development, conserved secondary structures and
homology with homeotic genes from Antirrhinum and Arabidopsis.
Pnueli, L.; Abu-Abeid, M.; Zamir, D.; Nacken, W.; Schwarz-
Sommer, Z.; Lifschitz, E.
Oxford : Blackwell Scientific Publishers and BIOS Scientific
Publishers; 1991 Sep.
The plant journal v. 1 (2): p. 255-266. ill; 1991 Sep.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Amino acid sequences;
Flowering; Gene expression; Nucleotide sequences; Restriction
mapping; Antirrhinum; Arabidopsis
115 NAL Call. No.: QK725.P532
A meristem-related gene from tomato encodes a dUTPase:
analysis of expression in vegetative and floral meristems.
Pri-Hadash, A.; Hareven, D.; Lifschitz, E.
Rockville, Md. : American Society of Plant Physiologists; 1992
Feb. The Plant cell v. 4 (2): p. 149-159; 1992 Feb. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Acid anhydride
hydrolases; Deoxyuridine; Nucleotide sequences; Amino acid
sequences; Apical meristems; Flowers; Cell differentiation;
Flowering; Mutants; Gene expression; Enzyme activity
Abstract: A meristem-specific gene coding for deoxyuridine
triphosphatase (EC 3.6.1.23) (dUTPase) in tomato was isolated,
and its developmental expression in vegetative and floral
apices was monitored. An 18-kD polypeptide, P18, was isolated
as a consequence of its accumulation in arrested floral
meristems of anantha mutant plants. The corresponding cDNA
isolated from an expression library exhibited a 40 to 60%
similarity with the pseudoprotease sequences of poxviruses,
genes that have been suggested to encode dUTPases. Enzymatic
tests and conservation of peptide motifs common to bacterial
and viral genes verified that the P18 cDNA clone indeed
represents a eukaryotic dUTPase. Immunogold localization and
in situ hybridization experiments showed that polypeptides and
transcripts of dUTPase are maintained at high levels in apical
meristematic cells of vegetative and floral meristems. dUTPase
gene activity is also high in the potentially meristematic
cells of the provascular and vascular system. Its expression
is lower in the immediate parenchymal derivatives of the
apical meristematic cells, and this downregulation marks,
perhaps, the transition from totipotency to the first
differentiated state.
116 NAL Call. No.: QK710.P62
Microprojectile bombardment of plant tissues increases
transformation frequency by Agrobacterium tumefaciens.
Bidney, D.; Scelonge, C.; Martich, J.; Burrus, M.; Sims, L.;
Huffman, G. Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 301-313; 1992 Jan. Includes references.
Language: English
Descriptors: Nicotiana tabacum; Helianthus annuus;
Agrobacterium tumefaciens; Genetic transformation; Mechanical
damage; Plant tissues; Reporter genes; Beta-glucuronidase;
Phosphotransferases; Gene expression; Kanamycin; Leaves;
Apical meristems
Abstract: Bombardment of plant tissues with microprojectiles
in an effective method of wounding to promote Agrobacterium-
mediated transformation. Tobacco cv. Xanthi leaves and
sunflower apical meristems were wounded by microprojectile
bombardment prior to application of Agrobacterium tumefaciens
strains containing genes within the T-DNA encoding GUS or
NPTII. Stable kanamycin-resistant tobacco transformants were
obtained using an NPTII construct from particle/plasmid,
particle-wounded/Agrobacterium-treated or scalpel-
wounded/Agrobacterium-treated potato leaves. Those leaves
bombarded with particles suspended in TE buffer prior to
Agrobacterium treatment produced at least 100 times more
kanamycin-resistant colonies than leaves treated by the
standard particle gun transformation protocol. In addition,
large sectors of GUS expression, indicative of meristem cell
transformation, were observed in plants recovered from
sunflower apical explants only when the meristems were wounded
first by particle bombardment prior to Agrobacterium
treatment. Similar results in two different tissue types
suggest that (1) particles may be used as a wounding mechanism
to enhance Agrobacterium transformation frequencies, and (2)
Agrobacterium mediation of stable transformation is more
efficient than the analogous particle/plasmid protocol.
117 NAL Call. No.: QK710.A9
Modification of gene expression in ripening fruit.
Speirs, J.; Brady, C.J.
East Melbourne : Commonwealth Scientific and Industrial
Research Organization; 1991.
Australian journal of plant physiology v. 18 (5): p. 519-532;
1991. Literature review. Includes references.
Language: English
Descriptors: Plant physiology; Fruits; Ripening; Genetic
regulation; Gene expression; Ethylene production; Enzyme
activity; Literature reviews
118 NAL Call. No.: QK710.P62
Molecular basis for novel root phenotypes induced by
Agrobacterium rhizogenes A4 on cucumber.
Amselem, J.; Tepfer, M.
Dordrecht : Kluwer Academic Publishers; 1992 Jun.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(3): p. 421-432; 1992 Jun. Includes references.
Language: English
Descriptors: Cucumis sativus; Agrobacterium rhizogenes;
Genetic transformation; Stems; Explants; Roots; Phenotypes;
Plant morphology; Tissue culture; Dna; Plasmids; Restriction
mapping; Genes; Gene expression; Messenger RNA; Molecular
mapping
Abstract: We have used the wild-type Agrobacterium rhizogenes
strain A4 to induce roots on cucumber stem explants. Cultures
of transformed roots obtained that were capable of hormone-
autonomous growth could be grouped in three phenotypic
classes. Of particular interest were extremely thick roots of
a type not previously described. Characterization of the
transferred DNA and of the expression of the corresponding
genes allowed us to determine that the genes rolABC of the TL
region of the Ri plasmid are sufficient to induce thin roots
similar to those observed in other species, while the aux
genes of the TR region are sufficient to induce thick roots.
Among clones bearing the aux genes, there was a correlation
between level of expression of aux2 and root phenotype.
119 NAL Call. No.: QK710.P62
Molecular biology of fruit ripening and its manipulation with
antisense genes. Gray, J.; Picton, S.; Shabbeer, J.; Schuch,
W.; Grierson, D. Dordrecht : Kluwer Academic Publishers; 1992
May.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(1): p. 69-87; 1992 May. Literature review. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Gene expression; Fruits;
Ripening; Messenger RNA; Antisense RNA; Genetic regulation;
Polygalacturonase; Pectinesterase; Ligases; Genes;
Oxidoreductases; Ethylene production; Literature reviews
Abstract: Considerable progress in tomato molecular biology
has been made over the past five years. At least 19 different
mRNAs which increase in amount during tomato fruit ripening
have been cloned and genes for enzymes involved in cell wall
degradation (polygalacturonase and pectinesterase) and
ethylene synthesis (ACC synthase) have been identified by
conventional procedures. Transgenic plants have been used to
identify regions of DNA flanking fruit-specific, ripening-
related and ethylene-regulated genes and trans-acting factors
which bind to these promoters have also been identified.
Antisense genes expressed in transgenic plants have proved to
be highly effective for inhibiting the specific expression of
ripening-related genes. These experiments have changed our
understanding of how softening occurs in tomato fruit.
Antisense techniques have also been used to identify genes
encoding enzymes for carotenoid biosynthesis (phytoene
synthase) and ethylene biosynthesis (the ethylene-forming
enzyme). The altered characteristics of fruit transformed with
specific antisense genes, such as retarded ripening and
resistance to splitting, may prove to be of value to fruit
growers, processors and ultimately the consumer.
120 NAL Call. No.: 385 J822
Molecular cloning and expression in Escherichia coli of cDNA
encoding the subunit of sweet potato beta-amylase.
Yoshida, N.; Nakamaura, K.
Tokyo : Japanese Biochemical Society; 1991 Aug.
Journal of biochemistry v. 110 (2): p. 196-201; 1991 Aug.
Includes references.
Language: English
Descriptors: Ipomoea batatas; Beta-amylase; Gene expression;
Cloning; Nucleotide sequences; Amino acid sequences;
Polypeptides
Abstract: Tuberous roots of the sweet potato are unusually
rich in beta-amylase, and the beta-amylase polypeptides
account for about 5% of the total soluble protein of the
organ. Unlike beta-amylases from other origins, the sweet
potato beta-amylase is a tetramer of identical subunits, and
it also bears starch phosphorylase-inhibitor activity. A cDNA
for the subunit of sweet potato beta-amylase was obtained by
immunological screening of an expression cDNA library
constructed by the vector-primer and linker method using a
plasmid vector containing tac-SP6 promoters. The SP6
transcript of a 2,000 base-pair-long cDNA insert directed the
synthesis in vitro of a precursor to the subunit of beta-
amylase which was identical in size with the mature subunit,
and the beta-amylase mRNA detected by Northern blot
hybridization was identical in size with the SP6 transcript of
the cDNA insert. The cDNA insert contained 1,494 base pairs of
an open reading frame which codes for the 499-amino-acid-long
precursor to the subunit of beta-amylase. An amino acid
sequence identical to the N-terminal amino acid sequence of
the mature subunit appeared immediately after the initiator
methionine of the precursor, indicating that the subunit of
beta-amylase is synthesized as a mature form. Comparison of
the amino acid sequences of subunits of sweet potato beta-
amylase and seed beta-amylases from barley and soybean
indicated that these enzymes share about 68% amino acid
identities among each other. Escherichia coli cells harboring
the cDNA clone produced the mature-sized subunit of the beta-
amylase, and the soluble extract exhibited amylolytic activity
which migrated to the same position as the beta-amylase
purified from the sweet potato in non-denaturing
polyacrylamide gel containing soluble starch indicating that
oligomerization of the subunit occurred properly in E. coli
cells.
121 NAL Call. No.: 500 N21P
Molecular cloning and expression in photosynthetic bacteria of
a soybean cDNA coding for phytoene desaturase, an enzyme of
the carotenoid biosynthesis pathway.
Bartley, G.E.; Viitanen, P.V.; Pecker, I.; Chamovitz, D.;
Hirschberg, J.; Scolnik, P.A.
Washington, D.C. : The Academy; 1991 Aug01.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (15): p. 6532-6539; 1991 Aug01.
Includes references.
Language: English
Descriptors: Glycine max; Glycine soja; Amino acid sequences;
Carotenoids; Cloning; Dna; Gene expression; Gene mapping;
Nucleotide sequences; Restriction fragment length polymorphism
Abstract: Carotendoids are orange, yellow, or red
photoprotective pigments present in all plastids. The first
carotenoid of the pathway is phytoene, a colorless compound
that is converted into colored carotenoids through a series of
desaturation reactions. Genes coding for carotenoid
desaturases have been cloned from microbes but not from
plants. We report the cloning of a cDNA for pds1, a soybean
(Glycine max) gene that, based on a complementation assay
using the photosynthetic bacterium Rhodobacter capsulatus,
codes for an enzymic that catalyzes the two desaturation
reactions that convert phytoene into zeta-carotene, a yellow,
carotenoid. The 2281-base-pair cDNA clone analyzed contains an
open reading frame with the capacity to code for a 572-residue
protein of predicted Mr 63,851. Alignment of the deduced Pds1
peptide sequence with the sequences of fungal and bacterial
carotenoid desaturases revealed conservation of several amino
acid residues, including a dinucleotide-binding motif that
could mediate binding to FAD. The Pds1 protein is synthesized
in vitro as a precursor that, upon import into isolated
chloroplasts, is processed to a smaller mature form.
Hybridization of the pds1 cDNA to genomic blots indicated that
this gene is a member of a low-copy-number gene family. One of
them loci was genetically mapped using restriction fragment
length polymorphisms between Glycine max and Glycine soja. We
conclude that pds1 is a nuclear gene encoding a phytoene
desaturase enzyme that, as its microbial counterparts,
contains sequence motifs characteristic of flavoproteins.
122 NAL Call. No.: QK710.P62
Molecular cloning, nuclear gene structure, and developmental
expression of NADPH: protochlorophyllide oxidoreductase in pea
(Pisum sativum L.). Spano, A.J.; He, Z.; Michel, H.; Hunt,
D.F.; Timko, M.P.
Dordrecht : Kluwer Academic Publishers; 1992 Mar.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(5): p. 967-972; 1992 Mar. Includes references.
Language: English
Descriptors: Pisum sativum; Genes; Oxidoreductases;
Protochlorophyllides; Nadph; Nucleotide sequences; Amino acid
sequences; Introns; Dna; Messenger RNA; Gene expression;
Etiolation; Light; Leaves
Abstract: Complementary DNA clones and a corresponding
nuclear gene (lpcr) encoding the NADPH-dependent
protochlorophyllide oxidoreductase (pchlide reductase, EC
1.6.99.1) have been characterized from pea (Pisum sativum L.).
The pea lpcr gene encodes a 43,118 Da precursor polypeptide
comprised of a transit peptide of 64 amino acids and a mature
protein of 336 amino acids. The coding portion of the gene is
interrupted by four introns, two of which are located within
the transit peptide coding portion of the gene. The deduced
primary structure for the pea protein is similar to those
reported for Arabidopsis and two monocot species. Northern
blot analysis revealed little to no decrease in steady-state
levels of mRNA encoding the enzyme in etiolated leaves
illuminated with continuous white light for up to 48 h. In
contrast, western blot analysis showed that the major
immunoreactive species present in whole leaf extracts
decreased to nearly undetectable levels during this same 48 h
period. These results suggest that pchlide reductase activity
in pea is primarily regulated post-transcriptionally, most
likely at the level of translation initiation/elongation or
protein turnover.
123 NAL Call. No.: QK710.P62
Molecular cloning of an 1-aminocyclopropane-1-carboxylate
synthase from senescing carnation flower petals.
Park, K.Y.; Drory, A.; Woodson, W.R.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 377-386; 1992 Jan. Includes references.
Language: English
Descriptors: Dianthus caryophyllus; Genes; Cloning; Ligases;
Acc; Nucleotide sequences; Amino acid sequences; Restriction
mapping; Gene expression; Messenger RNA; Corolla; Senescence;
Ethylene production; Abiotic injuries
Abstract: Synthetic oligonucleotides based on the sequence of
1-aminocyclopropane-1-carboxylate (ACC) synthase from tomato
were used to prime the synthesis and amplification of a 337 bp
tomato ACC synthase cDNA by polymerase chain reaction (PCR).
This PCR product was used to screen a cDNA library prepared
from mRNA isolated from senescing carnation flower petals. Two
cDNA clones were isolated which represented the same mRNA. The
longer of the two clones (CARACC3) contained a 1950 bp insert
with a single open reading frame of 516 amino acids encoding a
protein of 58 kDa. The predicted protein from the carnation
ACC synthase cDNA was 61%, 61%, 64%, and 51% identical to the
deduced proteins from zucchini squash, winter squash, tomato,
and apple, respectively. Genomic DNA gel blot analysis
indicated the presence of at least a second gene in carnation
which hybridized to CARACC3 under conditions of low
stringency. ACC synthase mRNA accumulates during senescence of
carnation flower petals concomitant with the increase in
ethylene production and ACC synthase enzyme activity. Ethylene
induced the accumulation of ACC synthase mRNA in presenescent
petals. Wound-induced ethylene production in leaves was not
associated with an increase in ACC synthase mRNA represented
by CARACC3. These results indicate that CARACC3 represents an
ACC synthase transcript involved in autocatalytic ethylene
production in senescing flower petals.
124 NAL Call. No.: 450 P692
Molecular cloning of tomato pectin methylesterase gene and its
expression in Rutgers, ripening inhibitor, nonripening, and
never ripe tomato fruits. Harriman, R.W.; Tieman, D.M.; Handa,
A.K.
Rockville, Md. : American Society of Plant Physiologists; 1991
Sep. Plant physiology v. 97 (1): p. 80-87; 1991 Sep. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Fruits; Ripening;
Pectins; Esterases; Enzyme activity; Genetic regulation;
Genetic code; Cloning; Gene expression; Extraction;
Purification; Nucleotide sequences
Abstract: We have purified pectin methylesterase (PME; EC
3.1.11) from mature green (MG) tomato (Lycopersicon esculentum
Mill. cv Rutgers) pericarp to an apparent homogeneity, raised
antibodies to the purified protein, and isolated a PME cDNA
clone from a lambda gtll expression library constructed from
MG pericarp poly(A)+ RNA. Based on DNA sequencing, the PME
cDNA clone isolated in the present study is different from
that cloned earlier from cv Ailsa Craig (J Ray et al. [1989]
Eur J Biochem 174:119-124). PME antibodies and the cDNA clone
are used to determine changes in PME gene expression in
developing fruits from normally ripening cv Rutgers and
ripening-impaired mutants ripening inhibitor (rin),
nonripening (nor), and never ripe (Nr). In Rutgers, PME mRNA
is first detected in 15-day-old fruit, reaches a steady-state
maximum between 30-day-old fruit and MG stage, and declines
thereafter. PME activity is first detectable at day 10 and
gradually increases until the turning stage. The increase in
PME activity parallels an increase in PME protein; however,
the levels of PME protein continue to increase beyond the
turning stage while PME activity begins to decline. Patterns
of PME gene expression in nor and Nr fruits are similar to the
normally ripening cv Rutgers. However, the rin mutation has a
considerable effect on PME gene expression in tomato fruits.
PME RNA is not detectable in rin fruits older than 45 days and
PME activity and protein begin showing a decline at the same
time. Even though PME activity levels comparable to 25-day-old
fruit were found in root tissue of normal plants, PME protein
and mRNA are not detected in vegetative tissues using PME
antibodies and cDNA as probes. Our data suggest that PME
expression in tomato pericarp is highly regulated during fruit
development and that mRNA synthesis and stability, protein
stability, and delayed protein synthesis influence the level
of PME activity in developing fruits.
125 NAL Call. No.: 381 J824
Molecular cloning to hyoscyamine 6 beta-hydroxylase, a
2-oxoglutarate-dependent dioxygenase, from cultured roots of
Hyoscyamus niger. Matsuda, J.; Okabe, S.; Hashimoto, T.;
Yamada, Y.
Baltimore, Md. : American Society for Biochemistry and
Molecular Biology; 1991 May25.
The Journal of biological chemistry v. 266 (15): p. 9460-9464;
1991 May25. Includes references.
Language: English
Descriptors: Hyoscyamus niger; Roots; Tropane alkaloids;
Oxygenases; Gene expression; Cloning; Dna; Nucleotide
sequences
Abstract: Roots of several solanaceous plants produce
anticholinergic alkaloids, hyoscyamine and scopolamine.
Hyoscyamine 6-beta-hydroxylase, a 2-oxoglutarate-dependent
dioxygenase (EC 1.14.11.11), catalyzes hydroxylation of
hyoscyamine in the biosynthetic pathway leading to
scopolamine. We report here on the isolation of cDNA clones
encoding the hydroxylase from a cDNA library made from mRNA of
the cultured roots of Hyoscyamus niger. The library was
screened with three synthetic oligonucleotides that encode
amino acid sequences of internal peptide fragments of the
purified hydroxylase. Nucleotide sequence analysis of the
cloned cDNA revealed an open reading frame that encodes 344
amino acids (Mr = 38,999). All 12 internal peptide fragments
determined in the purified enzyme were found in the amino acid
sequence deduced from the cDNA. With computer-aided comparison
to other proteins we found that the hydroxylase is homologous
to two synthases involved in the biosynthesis of beta-lactam
antibiotics in some microorganisms and the gene products of
tomato pTOM13 cDNA and maize A2 locus which had been proposed
to catalyze oxidative reactions in the biosynthesis of
ethylene and anthocyan, respectively. RNA blotting
hybridization showed that mRNA of the hydroxylase is abundant
in cultured roots and present in plant roots, but absent in
leaves, stems, and cultured cells of H. niger.
126 NAL Call. No.: QK710.P62
Molecular details of tomato extensin and glycine-rich protein
gene expression. Showalter, A.M.; Butt, A.D.; Kim, S.
Dordrecht : Kluwer Academic Publishers; 1992 May.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(2): p. 205-215; 1992 May. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Multigene families;
Glycoproteins; Plant proteins; Glycine; Hydroxyproline; Gene
expression; Transcription; Dna; Messenger RNA; Genetic
regulation; Ethylene; Water stress; Abscisic acid; Abiotic
injuries; Stems; Leaves; Cell wall components
Abstract: In a recent publication (Plant Molecular Biology
16: 547-565 (1991)), Showalter et al. described the isolation
and initial characterization of fifteen extensin and extensin-
like tomato cDNAs. These cDNAs were determined to fall into
five distinct classes; class I and II clones encoded
extensins, class III and V clones encoded glycine-rich
proteins (GRPs), and class IV clones encoded a portion of a
GRP sequence on one DNA strand and a portion of an extensin
sequence on the other DNA strand. In this publication, a more
detailed analysis of the expression of these cDNA classes was
performed with respect to wounding in various tomato organs,
development, kinetics and systemic extent of the wound
response, ethylene treatment, abscisic acid (ABA) treatment,
and drought stress by using RNA gel blot hybridizations. In
general, extensin gene expression was readily detected in
stems and roots, but not in leaves. With both class I and II
extensin cDNA probes, wound-induced accumulation of mRNA in
stems was first detected between 4 and 8 h after wounding with
maximal accumulation occurring after 12 h. Moreover, these
extensin wound responses were detected locally at the wound
site but not systemically. Expression of the class III GRP was
largely limited to wounded stem tissue. Initial detection and
maximal accumulation of the class III GRP mRNA was similar to
the extensins mRNAs; however, this GRP wound response occurred
both locally and systemically. Additionally, abscisic acid
treatment and drought stress resulted in the marked
accumulation of the class III GRP mRNA in tomato stems, but
did not alter the expression of the other cDNA classes. In
contrast, expression of the class V GRP occurred in stems and
roots and to a lesser extent in leaves and decreased in
response to wounding over a 24 h time period. The class V GRP
wound response was further characterized by an early,
transient accumulation of mRNA occurring 2-4 h after wounding
in stems and by its local nature.
127 NAL Call. No.: 448.3 J82
Mutation of the miaA gene of Agrobacterium tumefaciens results
in reduced vir gene expression.
Gray, J.; Wang, J.; Gelvin, S.B.
Washington, D.C. : American Society for Microbiology; 1992
Feb. Journal of bacteriology v. 174 (4): p. 1086-1098; 1992
Feb. Includes references.
Language: English
Descriptors: Agrobacterium tumefaciens; Genes; Mutations;
Virulence; Gene expression; Nucleotide sequences; Amino acid
sequences
Abstract: vir regulon expression in Agrobacterium tumefaciens
involves both chromosome- and Ti-plasmid-encoded gene
products. We have isolated and characterized a new chromosomal
gene that when mutated results in a 2- to 10-fold reduction in
the induced expression of vir genes by acetosyringone. This
reduced expression occurs in AB minimal medium (pH 5.5)
containing either sucrose or glucose and containing phosphate
at high or low concentrations. The locus was cloned and used
to complement A. tumefaciens strains harboring Tn5 insertions
in the gene. Sequence analysis of this locus revealed an open
reading frame with strong homology to the miaA locus of
Escherichia coli and the mod5 locus of Saccharomyces
cerevisiae. These genes encode tRNA: isopentenyltransferase
enzymes responsible for the specific modification of the A-37
residue in UNN codon tRNA species. The function of the
homologous gene in A. tumefaciens was proven by genetic
complementation of E. coli miaA mutant strains. tRNA
undermodification in A. tumefaciens miaA mutant strains may
reduce vir gene expression by causing a reduced translation
efficiency. A slight reduction in the virulence of these
mutant Agrobacterium strains on red potato plants, but not on
tobacco, tomato, kalanchoe, or sunflower plants, was observed.
128 NAL Call. No.: SB732.6.M65
Nodulin regulation in common bean nodules induced by bacterial
mutants. Padilla, J.E.; Miranda, J.; Sanchez, F.
St. Paul, Minn. : APS Press; 1991 Sep.
Molecular plant-microbe interactions : MPMI v. 4 (5): p.
433-439; 1991 Sep. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Nitrogen fixation; Rhizobium
leguminosarum; Agrobacterium; Strains; Mutants; Root nodules;
Nodulins; Genes; Genetic regulation; Gene expression;
Symbiosis; Nodulation
129 NAL Call. No.: QK710.P62
Nuclear factors binding to the extensin promoter exhibit
differential activity in carrot protoplasts and cells.
Granell, A.; Pereto, J.G.; Schindler, U.; Cashmore, A.R.
Dordrecht : Kluwer Academic Publishers; 1992 Feb.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(4): p. 739-748; 1992 Feb. Includes references.
Language: English
Descriptors: Daucus carota; Dna binding proteins; Binding
site; Promoters; Glycoproteins; Cell wall components;
Protoplasts; Deletions; Controlling elements; Transcription;
Gene expression; Binding proteins; Abiotic injuries;
Nucleotide sequences
Abstract: The expression of the cell wall protein extensin, a
hydroxyproline-rich glycoprotein, is induced by several
different stimuli, including wounding. The process of
protoplast preparation mimics the wounding effect and results
in the induction of extensin. Using transient expression in
protoplasts we analyzed several deletions of the extensin
promoter. We identified an important transcriptional
regulatory element located between the two TATA boxes that
characterize the extensin promoter. Other regulatory elements,
located further upstream between -719 to -658, are necessary
for maximum level of expression. Employing electrophoretic
mobility shift assays and methylation interference
experiments, we demonstrate the interaction of nuclear factors
with these upstream regulatory elements. In addition to the
previously identified factors EGBF-1 and EGBF-2, which are
mainly present in unwounded cells, we identified an additional
novel DNA-binding activity that is present in extracts
prepared from protoplasts but not in extracts from unwounded
cells. This factor, designated EBF (extensin-binding protein),
binds to a DNA fragment which when deleted results in a 48%
reduction in expression.
130 NAL Call. No.: QK710.P68
A nuclear protein binding to dA/dT-rich sequences upstream
from the radish DNA promoter.
Echeverria, M.; Delcasso-Tremousaygue, D.; Delseny, M.
Oxford : Blackwell Scientific Publishers and BIOS Scientific
Publishers; 1992 Mar.
The plant journal v. 2 (2): p. 211-219; 1992 Mar. Includes
references.
Language: English
Descriptors: Raphanus sativus; Nuclei; Rna; Dna; Gene mapping;
Promoters; Binding proteins; Transcription; Rna polymerase;
Enzyme activity; Gene expression; Protein composition; Protein
content; Nucleotide sequences
131 NAL Call. No.: QK710.P62
Nucleotide sequence and expression of the ribosomal protein L2
gene in pea chloroplasts.
Nagano, Y.; Ishikawa, H.; Matsuno, R.; Sasaki, Y.
Dordrecht : Kluwer Academic Publishers; 1991 Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 541-545; 1991 Sep. Includes references.
Language: English
Descriptors: Pisum sativum; Genes; Ribosomes; Nucleoproteins;
Cloning; Nucleotide sequences; Gene expression; Chloroplasts;
Dna; Chloroplast genetics; Messenger RNA; Greening; Seedlings
Abstract: We sequenced the nucleotides around the rpl2 gene,
encoding the ribosomal protein L2, in pea (Pisum sativum cv.
Alaska) chloroplasts and analyzed the expression of the rpl2
gene. During deetiolation, accumulation of the rpl2 transcript
did not require de novo protein synthesis on chloroplastic
ribosomes, in contrast to that of most chloroplast-encoded
genes. This suggested that the mechanism involved in the
expression of rpl2 differed from that of most chloroplast-
encoded genes.
132 NAL Call. No.: 450 P692
Nucleotide sequence and spatial expression pattern of a
drought- and abscisic acid-induced gene of tomato.
Plant, A.L.; Cohen, A.; Moses, M.S.; Bray, E.A.
Rockville, Md. : American Society of Plant Physiologists; 1991
Nov. Plant physiology v. 97 (3): p. 900-906; 1991 Nov.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Gene expression;
Nucleotide sequences; Amino acid sequences; Drought; Abscisic
acid; Genetic regulation
Abstract: The nucleotide sequence of le16, a tomato
(Lycopersicon esculentum Mill.) gene induced by drought stress
and regulated by abscisic acid specifically in aerial
vegetative tissue, is presented. The single open reading frame
contained within the gene has the capacity to encode a
polypeptide of 12.7 kilodaltons and is interrupted by a small
intron. The predicted polypeptide is rich in leucine, glycine,
and alanine and has an isoelectric point of 8.7. The amino
terminus is hydrophobic and characteristic of signal sequences
that target polypeptides for export from the cytoplasm. There
is homology (47.2% identity) between the amino terminus of the
LE16 polypeptide and the corresponding amino terminal domain
of the maize phospholipid transfer protein. le16 was expressed
in drought-stressed leaf, petiole, and stem tissue and to a
much lower extent in the pericarp of mature green tomato fruit
and developing seeds. No expression was detected in the
pericarp of red fruit or in drought-stressed roots. Expression
of le16 was also induced in leaf tissue by a variety of other
abiotic stresses including polyethylene glycol-mediated water
deficit, salinity, cold stress, and heat stress. None of these
stresses or direct applications of abscisic acid induced the
expression of le16 in the roots of the same plants. The unique
expression characteristics of this gene indicates that novel
regulatory mechanisms, in addition to endogenous abscisic
acid, are involved in controlling gene expression.
133 NAL Call. No.: QK710.P62
Nucleotide sequence of a tobacco cDNA encoding plastidic
glutamine synthetase and light inducibility, organ specificity
and diurnal rhythmicity in the expression of the corresponding
genes of tobacco and tomato. Becker, T.W.; Caboche, M.;
Carrayol, E.; Hirel, B.
Dordrecht : Kluwer Academic Publishers; 1992 Jun.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(3): p. 367-379; 1992 Jun. Includes references.
Language: English
Descriptors: Nicotiana tabacum; Lycopersicon esculentum;
Structural genes; Multiple genes; Glutamate-ammonia ligase;
Nucleotide sequences; Dna; Amino acid sequences; Gene
expression; Transcription; Messenger RNA; Genetic regulation;
Phytochrome; White light; Red light; Far red light; Diurnal
variation; Leaves; Cotyledons; Stems; Roots
Abstract: A full-length cDNA encoding glutamine synthetase
(GS) was cloned from a lambda-gt10 library of tobacco leaf
RNA, and the nucleotide sequence was determined. An open
reading frame accounting for a primary translation product
consisting of 432 amino acids has been localized on the cDNA.
The calculated molecular mass of the encoded protein is 47.2
kDa. The predicted amino acid sequence of this precursor shows
higher homology to GS-2 protein sequences from other species
than to a leaf GS-1 polypeptide sequence, indicating that the
cDNA isolated encodes the chloroplastic isoform (GS-2) of
tobacco GS. The presence of C- and N-terminal extensions which
are characteristic of GS-2 proteins supports this conclusion.
Genomic Southern blot analysis indicated that GS-2 is encoded
by a single gene in the diploid genomes of both tomato and
Nicotiana sylvestris, while two GS-2 genes are very likely
present in the amphidiploid tobacco genome. Western blot
analysis indicated that in etiolated and in green tomato
cotyledons GS-2 subunits are represented by polypeptides of
similar size, while in green tomato leaves an additional GS-2
polypeptide of higher apparent molecular weight is detectable.
In contrast, tobacco GS-2 is composed of subunits of identical
size in all organs examined. GS-2 transcripts and GS-2
proteins could be detected at high levels in the leaves of
both tobacco or tomato. Lower amounts of GS-2 mRNA were
detected in stems, corolla, and roots of tomato, but not in
non-green organs of tobacco. The GS-2 transcript abundance
exhibited a diurnal fluctuation in tomato leaves but not in
tobacco leaves. White or red light stimulated the accumulation
of GS-2 transcripts and GS-2 protein in etiolated tomato
cotyledons. Far-red light cancelled this stimulation. The red
light response of the GS-2 gene was reduced in etiolated
seedlings of the phytochrome-deficient aurea mutant of tomato.
These results indicate a phytochrome-mediated light
stimulation of GS-2 gene expression d
134 NAL Call. No.: QK710.P62
Nucleotide sequence of an ABA-induced tomato gene that is
expressed in wilted vegetative organs and developing seeds.
Cohen, A.; Bray, E.A.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 411-413; 1992 Jan. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Nucleotide
sequences; Amino acid sequences; Plant proteins; Gene
expression; Genetic regulation; Abscisic acid; Wilting; Seed
development; Water stress; Leaves
135 NAL Call. No.: QK710.P62
Organization and expression of the nuclear gene coding for the
plastid-specific S22 ribosomal protein from spinach.
Bisanz-Seyer, C.; Mache, R.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 337-344; 1992 Jan. Includes references.
Language: English
Descriptors: Spinacia oleracea; Genes; Ribosomes; Proteins;
Introns; Exons; Nucleotide sequences; Gene expression;
Messenger RNA; Promoters; Leaves; Roots; Seeds; Seed
germination; Plastids; Amino acid sequences
Abstract: We report here on the genomic organization and
expression of a nuclear gene coding for a plastid ribosomal
protein. The gene encodes the plastid-specific ribosomal
protein S22 (formerly named CS-S5). Southern blot analysis
suggests that the gene is present in one copy in the spinach
genome. The gene consists of 5 exons of sizes ranging from 108
to 273 bp and of 4 introns of 1410, 92, 386 and 82 bp. The
exon-intron splice junctions and intron branch sites fit well
the consensus sequences for plant introns. The major
transcription start site has been determined 29 bp upstream of
the AUG initiation codon by primer extension and S1 nuclease
mapping. No canonical TATA box is found but some other
possible promoter motifs are observed. Transcripts are
detected in leaves, etiolated leaves, roots and seeds
suggesting that the rps22 gene is expressed constitutively.
During germination a marked increase in the relative steady-
state level of the mRNA can be seen as soon as 24 h after
imbibition of the seeds.
136 NAL Call. No.: 450 P692
Organ-specific and environmentally regulated expression of two
abscisic acid-induced genes of tomato. Nucleotide sequence and
analysis of the corresponding cDNAs.
Cohen, A.; Plant, A.L.; Moses, M.S.; Bray, E.A.
Rockville, Md. : American Society of Plant Physiologists; 1991
Dec. Plant physiology v. 97 (4): p. 1367-1374; 1991 Dec.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Gene expression; Genetic
regulation; Abscisic acid; Water stress; Drought; Stress
response; Dna; Genetic code; Nucleotide sequences; Amino acid
sequences
Abstract: The cDNAs, pLE4 and pLE25, represent mRNAs that
accumulate in response to water deficit and elevated levels of
endogenous abscisic acid in detached leaves of drought-
stressed tomato (Lycopersicon esculentum Mill., cv Ailsa
Craig) (A Cohen, EA Bray [1990] Planta 182: 27-33). DNA
sequence analysis of pLE4 and pLE25 showed that the deduced
polypeptides were 13.9 and 9.3 kilodaltons, respectively. Each
polypeptide was hydrophilic, cysteine- and tryptophan-free,
and found to be similar to previously identified proteins that
accumulate during the late stages of embryogenesis. pLE4 and
pLE25 mRNA accumulated in a similar organ-specific pattern in
response to specific abiotic stresses. Yet, expression
patterns of the corresponding genes in response to
developmental cues were not similar. pLE25 mRNA accumulated to
much higher levels in developing seeds than in drought-
stressed vegetative organs. pLE4 mRNA accumulated
predominantly in drought-stressed leaves. The similarities and
differences in the accumulation characteristics of these two
mRNAs indicates that more than one mechanism exists for the
regulation of their corresponding genes.
137 NAL Call. No.: 385 J822
Organ-specific occurrence and expression of the isoforms of
nonspecific lipid transfer protein in castor bean seedlings,
and molecular cloning of a full-length cDNA for a cotyledon-
specific isoform.
Tsuboi, S.; Suga, T.; Takishima, K.; Mamiya, G.; Matsui, K.;
Ozeki, Y.; Yamada, M.
Tokyo : Japanese Biochemical Society; 1991 Nov.
Journal of biochemistry v. 110 (5): p. 823-831; 1991 Nov.
Includes references.
Language: English
Descriptors: Ricinus communis; Seedlings; Membranes; Lipids;
Transfer; Proteins; Purification; Amino acid sequences; Gene
expression; Cloning; Nucleotide sequences
Abstract: Four kinds of nonspecific lipid transfer proteins
(nsLTP) were purified from different organs of castor bean
(Ricinus communis L.) seedlings. Amino acid compositions and
amino-terminal sequences of the four nsLTPs were determined
and compared with those of castor bean isoforms, nsLTP-A, -B,
and -C, previously reported [Takishima et al. (1986) Biochim.
Biophys. Acta 870,248 255; Takishima et al. (1988) Eur. J.
Biochem. 177, 241-249]. Two isoforms from the cotyledons were
identified as nsLTP-A and -C, one isoform from the endosperms
as nsLTP-B, and the other was a new isoform from the axes.
This new isoform was named nsLTP-D and its amino acid sequence
was determined. These results demonstrated organ-specific
occurrence of the nsLTP isoforms in castor bean seedlings. The
isoforms nsLTP-A, -B, -C, and -D showed similar transfer
activity not only for phosphatidylcholine and
phosphatidylethanolamine but also for
monogalactosyldiacylglycerol, although the homology among
their amino acid sequences ranged from 70 to 30%. Two cDNA
clones (pnsLTP-C and pnsLTP-D) for nsLTPs of castor bean
seedlings were isolated and sequenced. pnsLTP-C was the cDNA
clone for nsLTP-C expressed in the cotyledons, and pnsLTP-D
was that for nsLTP-D in the axis. A coupled in vitro
transcription-translation analysis of both cDNA clones
revealed that pnsLTP-C encodes the full-length of nsLTP-C
precursor (pro-nsLTP-C), while pnsLTP-D encodes a part of
nsLTP-D precursor. Pro-nsLTP-C contained a 24 amino acid pre-
sequence preceding the mature nsLTP-C (92 amino acids).
Northern blot analyses of mRNAs from castor bean organs for
nsLTP-C and -D demonstrated the organ-specific expression of
nsLTPs; nsLTP-C was mainly expressed in the cotyledons and
nsLTP-D in the axis, although small amounts of nsLTP-C and
nsLTP-D were expressed in the axis and cotyledons,
respectively.
138 NAL Call. No.: QK710.P62
Patatin and four serine proteinase inhibitor genes are
differentially expressed during photo tuber development.
Hendriks, T.; Vreugdenhil, D.; Stiekema, W.J.
Dordrecht : Kluwer Academic Publishers; 1991 Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 385-394; 1991 Sep. Includes references.
Language: English
Descriptors: Solanum tuberosum; Multigene families;
Glycoproteins; Proteinase inhibitors; Serine proteinases;
Transcription; Gene expression; Plant development; Tubers;
Axils; Buds; Photoperiod; Tissue culture
Abstract: A highly efficient and synchronous in vitro
tuberization system is described. One-node stem pieces from
potato (Solanum tuberosum cv. Bintje) plants grown under short
day-light conditions containing an axillary bud were cultured
in the dark on a tuber-inducing medium. After 5 or 6 days all
axillary buds started to develop tubers. To study gene
expression during tuber development, RNA isolated from
tuberizing axillary buds was used for both in vitro
translation and northern blot hybridizations. The genes
encoding the proteinase inhibitors I and II (PI-I and PI-II),
a Kunitz- and a Bowman-Birk-type proteinase inhibitor were
already expressed in uninduced axillary buds. The length of
the day-light conditions differently influenced the expression
level of the individual genes. In addition, the expression of
each of these genes changed specifically during the
development of the axillary bud to tuber. In contrast to the
expression of these proteinase inhibitor genes, patatin gene
expression was only detectable from the day tuberization was
manifested as a radial expansion of the axillary bud. These
results are discussed with respect to the regulation of the
expression of the genes studied in relation to the regulation
of tuber development.
139 NAL Call. No.: QP501.B64
The pattern of plant annexin gene expression.
Smallwood, M.F.; Gurr, S.J.; McPherson, M.J.; Roberts, K.;
Bowles, D.J. London : The Biochemical Society; 1992 Jan15.
The Biochemical journal v. 281 (pt.2): p. 501-505; 1992 Jan15.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Solanum tuberosum;
Hordeum vulgare; Roots; Leaves; Stems; Cell suspensions; Plant
proteins; Dna; Rna; Gene expression
Abstract: Peptide sequence data derived from a plant annexin,
P34 [Smallwood, Keen & Bowles (1990) Biochem. J. 270, 157-161]
was used to design amplimers for PCR. A unique fragment of 95
bp, amplified from tomato (Lycopersicon esculentum) genomic
DNA, was used in Northern analyses and demonstrated a
differential pattern of expression in vegetative tissues of
tomato, potato (Solanum tuberosum) and barley (Hordeum
vulgare). The tissue-specific abundance of the annexin
transcript was found to correlate closely with abundance of
annexin protein as revealed by their partial purification and
analysis with antisera specific for annexins isolated from
tomato suspension-culture cells.
140 NAL Call. No.: QH301.J6
PCNA and total nuclear protein content as markers of cell
proliferation in pea tissue.
Citterio, S.; Sgorbati, S.; Levi, M.; Colombo, B.M.; Sparvoli,
E. Cambridge : The Company of Biologists Limited; 1992 May.
Journal of cell science v. 102 (pt.1): p. 71-78; 1992 May.
Includes references.
Language: English
Descriptors: Pisum sativum; Antigens; Cell growth; Dna; Gene
expression; Immunocytochemistry; Nucleoproteins; Seed
germination
141 NAL Call. No.: 442.8 Z8
PCR detection of transcripts homologous to the self-
incompatibility gene in anthers of Brassica.
Guilluy, C.M.; Trick, M.; Heizmann, P.; Dumas, C.
Berlin, W. Ger. : Springer International; 1991.
Theoretical and applied genetics v. 82 (4): p. 466-472; 1991.
Includes references.
Language: English
Descriptors: Brassica oleracea; Loci; Self incompatibility;
Messenger RNA; Polymerase chain reaction; Anthers;
Transcription; Gene expression; Leaves; Stigma; Roots
Abstract: The polymerase chain reaction (PCR) is particularly
well suited for the detection of rare sequences. Taking
advantage of the recent isolation of sequences associated with
stigma self-incompatibility in Brassica oleracea, we used PCR
amplifications with primers synthesized to the S6 cDNA
sequence, to demonstrate the presence of mRNA homologous to
stigma S-locus gene (SLG) in anthers during early
microsporogenesis. In addition, other S-locus-related (SLR)
sequences were shown to be transcribed in sexual as well as in
vegetative tissues (roots, leaves), suggesting that the SLG
family might be involved not only in pollen-stigma
recognition, but more generally in various forms of plant cell
signalling processes. This information corroborates the recent
discovery of a cDNA-deduced protein kinase from maize roots,
whose extracellular receptor displays high homology with
Brassica S-locus-specific glycoproteins.
142 NAL Call. No.: QK725.P532
The pea ferredoxin I gene exhibits different light responses
in pea and tobacco.
Gallo-Meagher, M.; Sowinski, D.A.; Thompson, W.F.
Rockville, Md. : American Society of Plant Physiologists; 1992
Apr. The Plant cell v. 4 (4): p. 383-388; 1992 Apr. Includes
references.
Language: English
Descriptors: Pisum sativum; Nicotiana tabacum; Genetic
transformation; Transgenics; Ferredoxin; Structural genes;
Gene expression; Phytochrome; Genetic regulation; Messenger
RNA; White light; Red light; Far red light; Photoreceptors;
Etiolation
Abstract: We monitored Fed-1 (encoding ferredoxin I) mRNA
levels in etiolated transgenic tobacco seedlings containing
the intact pea Fed-1 gene to determine if the characteristic
light responses of this gene in pea seedlings are also
observed in transgenic tobacco. Fed-1 transcript levels in
transgenic tobacco seedlings closely paralleled those of the
native gene in pea buds when etiolated seedlings were
transferred to white light. However, the response to red light
was much smaller in tobacco than in pea and was not
efficiently reversed by far-red light. The red light response
of endogenous tobacco ferredoxin transcripts is closely
comparable to that of the Fed-1 transgene, with a similar lack
of photoreversibility. Thus, the pea Fed-1 transgene responds
normally to tobacco gene-regulatory factors, but these
factor's are less influenced by phytochrome in tobacco
cotyledons than in pea buds.
143 NAL Call. No.: QH506.A1M622
Pea (Pisum sativum) genes involved in symbiosis with nitrogen-
fixing bacteria. I. Analysis of the expression of the early
nodulin gene ENOD12 using the polymerase chain reaction.
Zalenskii, A.O.; Kozik, A.V.; Scheres, V.; Bisseling, A.;
Tikhonovich, I.A. New York, N.Y. : Consultants Bureau; 1991
Dec.
Molecular biology v. 25 (3,pt.2): p. 638-644; 1991 Dec.
Translated from: Molekuliarnaia biologiia, v. 25 (3, pt. 2),
1991, p. 787-794. (QH506.A1M62). Includes references.
Language: English; Russian
Descriptors: Pisum sativum; Rhizobium leguminosarum; Genes;
Nodulins; Gene expression; Polymerase chain reaction;
Nodulation; Transcription; Genetic regulation; Root hairs;
Messenger RNA; Root nodules; Flavonoids
Abstract: The polymerase chain reaction (PCR) was used to
detect the transcription products of the early nodulin gene in
the pea. Single-stranded DNA copies were prepared using a
primer corresponding to the terminal part of a previously
sequenced cDNA clone and a total RNA isolate. The presence of
amplification products was detected using Southern
hybridization. Expression of the ENOD12 gene was found to
occur at the earliest developmental stages of the symbiosis
between the pea and nitrogen-fixing bacteria, and occurred in
root hair cell. Transcription activation required sufficient
levels of activity of a limited number of symbiotic bacterial
genes, namely nodDABC and nodE. Expression of ENOD12 was
inducible by a soluble component excreted into the medium by
activated bacteria, and by inhibitors of soluble hormone
(auxins) transport. The ENOD12 gene was shown to lack introns.
144 NAL Call. No.: QP501.E8
Phenylalanine amonia-lyase in potato (Solanum tuberosum L.).
Genomic complexity, structural comparison of two selected
genes and modes of expression.
Joos, H.J.; Hahlbrock, K.
New York, NY : Springer-Verlag New York Inc; 1992 Mar.
European journal of biochemistry v. 204 (2): p. 621-629; 1992
Mar. Includes references.
Language: English
Descriptors: Solanum tuberosum; Phenylalanine ammonia-lyase;
Structural genes; Messenger RNA; Dna; Clones; Genomes; Amino
acid sequences; Nucleotide sequences; Phytophthora infestans;
Injuries; Stress response; Gene expression
Abstract: Potato (Solanum tuberosum L. cv. Datura) contains
approximately 40-50 phenylalanine ammonia-lyase (PAL)
genes/haploid genome. Considerable cDNA heterogeneity
indicates that at least about 10, and probably more, of these
genes are potentially active. One subfamily, represented by
one selected member (PAL-1), was analyzed with respect to
genomic complexity, nucleotide and deduced amino acid
sequence, and mode of constitutive or induced expression. For
comparison, a second gene (PAL-2), representing several
subfamilies that are easily distinguished from PAL-1, was
included in these studies. Extensive structural similarities
were observed both between the TATA-proximal portions of the
PAL-1 and PAL-2 promoters, particularly in the areas
containing putative cis-acting elements, and among all
presently known PAL proteins from various higher and lower
plants. The relative abundance of PAL mRNA varied greatly in
several major potato organs. However, the patterns obtained
with probes detecting either total PAL mRNA or more
specifically, PAL-1-related or PAL-2-related mRNA species,
were the same within experimental error. Mature leaves
contained particularly low levels of PAL mRNA. Infection of
these leaves with the pathogenic fungus, Phytophthora
infestans, resulted in a large, transient induction of PAL
mRNA. The relative timing of PAL-1 and PAL-2 mRNA expression,
however, differed in compatible (fungus virulent, plant
susceptible) but not in incompatible interactions (fungus
avirulent, plant resistant). Wounding of leaves caused an
extremely rapid and transient induction of both PAL mRNA
species.
145 NAL Call. No.: QK725.P532
Phenylpropanoid pathway intermediates regulate transient
expression of a chalcone synthase gene promoter.
Loake, G.J.; Choudhary, A.D.; Harrison, M.J.; Mavandad, M.;
Lamb, C.J.; Dixon, R.A.
Rockville, Md. : American Society of Plant Physiologists; 1991
Aug. The Plant cell v. 3 (8): p. 829-840; 1991 Aug. Includes
references.
Language: English
Descriptors: Phaseolus vulgaris; Medicago sativa;
Colletotrichum lindemuthianum; Promoters; Naringenin-chalcone
synthase; Chloramphenicol acetyltransferase; Reporter genes;
Chimeras; Gene expression; Transcription; Genetic regulation;
Cinnamic acid; P-coumaric acid; Carbohydrates; Cell wall
components; Hyphae; Deletions; Genetic transformation;
Protoplasts; Electroporation
Abstract: A chimeric gene construct containing a bean
chalcone synthase (CHS) promoter fused to the chloramphenicol
acetyltransferase (CAT) reporter gene was strongly expressed
when electroporated into alfalfa protoplasts that were then
exposed to a fungal elicitor. Low concentrations (5 X 10(-6)
to 10(-4) M) of exogenously applied transcinnamic acid (CA),
the first intermediate of the phenylpropanoid pathway,
slightly stimulated elicitor-induced CAT expression, whereas
high concentrations (>1O(-4) M) severely reduced expression to
below the levels observed in the absence of elicitor. In
contrast, trans-p-coumaric acid (4-CA, the second intermediate
in the pathway) stimulated expression from the CHS promoter up
to 4.5-fold at 5 X 10(-4) M. Expression of CAT driven by the
promoters of other elicitor-inducible defense response genes
was not markedly affected by CA or 4-CA. Stimulation of CHS
promoter expression by low concentrations of CA and 4-CA was
completely abolished by 5' deletion to position -130, but not
-174. When the -180 to -130 region of the CHS15 promoter was
coelectroporated into elicited protoplasts on a separate
plasmid along with the intact -326 CHS-CAT construct, the
decreased CAT expression as a function of CA or 4-CA
concentration was consistent with the coelectroporated
sequence competing in trans with the intact promoter for the
binding of a factor(s) involved in the up regulation of CHS
transcription by 4-CA and low concentrations of CA. Our data
support the hypothesis that phenylpropanoid compounds may act
as natural and specific regulators of plant gene expression
and define the location of a cis-acting element in the CHS15
promoter involved in the induction by phenylpropanoid pathway
intermediates.
146 NAL Call. No.: 448.3 J82
Plant and environmental sensory signals control the expression
of hrp genes in Pseudomonas syringae pv. phaseolicola.
Rahme, L.G.; Mindrinos, M.N.; Panopoulos, N.J.
Washington, D.C. : American Society for Microbiology; 1992
Jun. Journal of bacteriology v. 174 (11): p. 3499-3507; 1992
Jun. Includes references.
Language: English
Descriptors: Pseudomonas syringae pv. phaseolicola; Genes;
Gene expression; Ph; Osmolarity; Amino acids; Fructose;
Sucrose; Succinic acid; Citrates; In vitro
Abstract: The hrp genes of Pseudomonas syringae pv.
phaseolicola control the development of primary disease
symptoms in bean plants and the elicitation of the
hypersensitive response in resistant plants. We examined the
expression of the seven operons located in the 22-kb hrp
cluster (L. G. Rahme, M. N. Mindrinos, and N. J. Panopoulos,
J. Bacteriol. 173:575-586, 1991) in planta and in vitro under
different physiological and nutritional conditions by using
chromosomally located hrp::inaZ reporter fusions. We show that
(i) a plant signal(s) is specifically required for the
induction of the seven hrp operons, during both compatible and
incompatible interactions; (ii) hrpL and hrpRS are regulated
by different mechanisms in planta and in vitro; and (iii)
expression of individual hrp loci is differentially affected
by pH, osmotic strength, and type of carbon source: hrpAB,
hrpC, and hrpD were downregulated similarly by osmolarity, pH,
and certain carbon sources; hrpE expression was affected
strongly by pH and carbon substrate and slightly by
osmolarity; and hrpF was not substantially affected by any of
these factors. These findings suggest complex signaling
mechanisms taking place during plant-pathogen interactions.
147 NAL Call. No.: 442.8 Z8
Plant cells selected for resistance to phosphate starvation
show enhanced P use efficiency.
Goldstein, A.H.
Berlin, W. Ger. : Springer International; 1991.
Theoretical and applied genetics v. 82 (2): p. 191-194; 1991.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; In vitro selection;
Phosphates; Mineral deficiencies; Resistance; Tissue culture;
Callus; Cell lines; Multigene families; Gene expression;
Genetic regulation; Somaclonal variation; Acid phosphatase;
Isoenzymes; Secretion; Nutrition physiology; Nutrient uptake;
Cell suspensions
Abstract: In many organisms, phosphate starvation induces
multigene systems that act to increase the availability and
uptake of exogenous phosphates. Tissue-cultured tomato cells
were plated onto solid media containing starvation levels of
phosphate. While most cells died, we identified isolated
clumps of callus capable of near-normal rates of growth.
Starvation-resistant cells were used to start suspension
cultures that were kept under phosphate starvation conditions.
A selected cell line showed constitutively enhanced secretion
of acid phosphatase and greatly increased rates of phosphate
uptake. These pleiotropic effects suggest modification of a
regulatory apparatus that controls coordinated changes in the
expression of a multigene system. The somaclonal variant cell
line grew normally under phosphate-sufficient conditions, but
did significantly better than unselected cells under
phosphate-limited conditions. In vitro selection may be a
useful system for developing phosphate ultraefficient crop
plants.
148 NAL Call. No.: QK725.P532
Plant enolase: gene structure, expression, and evolution.
Straeten, D. van der; Rodrigues-Pousada, R.A.; Goodman, H.M.;
Montagu, M. van Rockville, Md. : American Society of Plant
Physiologists; 1991 Jul. The Plant cell v. 7 (3): p. 719-735;
1991 Jul. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Arabidopsis thaliana;
Multigene families; Hydro-lyases; Cloning; Nucleotide
sequences; Amino acid sequences; Gene expression; Messenger
RNA; Roots; Leaves; Plant development; Introns; Exons;
Molecular conformation; Anaerobic conditions; Heat shock;
Chloroplast genetics; Genetic transformation; Escherichia
coli; Fruits; Ripening
Abstract: Enolase genes were cloned from tomato and
Arabidopsis. Comparison of their primary structures with other
enolases revealed a remarkable degree of conservation, except
for the presence of an insertion of 5 amino acids unique to
plant enolases. Expression of the enolase genes was studied
under various conditions. Under normal growth conditions,
steady-state messenger and enzyme activity levels were
significantly higher in roots than in green tissue. Large
inductions of mRNA, accompanied by a moderate increase in
enzyme activity, were obtained by an artificial ripening
treatment in tomato fruits. However, there was little effect
of anaerobiosis on the abundance of enolase messenger. In heat
shock conditions, no induction of enolase mRNA was observed.
We also present evidence that, at least in Arabidopsis, the
hypothesis that there exists a complete set of glycolytic
enzymes in the chloroplast is not valid, and we propose
instead the occurrence of a substrate shuttle in Arabidopsis
chloroplasts for termination of the glycolytic cycle.
149 NAL Call. No.: SB317.5.H6
Polygalacturonase and tomato fruit ripening.
Giovannoni, J.J.; DellaPenna, D.; Bennett, A.B.; Fischer, R.L.
Portland, Or. : Timber Press; 1992.
Horticultural reviews v. 13: p. 67-103; 1992. Literature
review. Includes references.
Language: English
Descriptors: Tomatoes; Lycopersicon esculentum; Fruits;
Ripening; Enzyme activity; Polygalacturonase; Literature
reviews; Cell walls; Isoenzymes; Enzyme polymorphism; Genes;
Gene expression; Genetic regulation; Transcription; Mutants;
Chimeras
150 NAL Call. No.: QH506.E46
Positive and negative cis-acting DNA domains are required for
spatial and temporal regulation of gene expression by a seed
storage protein promoter. Bustos, M.M.; Begum, D.; Kalkan,
F.A.; Battraw, M.J.; Hall, T.C. Oxford, Eng. : IRL Press; 1991
Jun.
The EMBO journal - European Molecular Biology Organization v.
10 (6): p. 1469-1479; 1991 Jun. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Nicotiana tabacum; Genetic
regulation; Gene expression; Phaseolin; Promoters; Beta-
glucuronidase; Reporter genes; Nucleotide sequences; Dna;
Transgenics; Embryogenesis; Cotyledons; Hypocotyls; Shoot
meristems; Temporal variation; Spatial variation; Seed
development
Abstract: Mutations affecting spatial and temporal regulation
of a beta-phaseolin gene encoding the major storage protein of
bean (Phaseolus vulgaris) were analyzed by stable and
transient transformation approaches. The results substantiate
the value of transient assays for rapid determination of the
functionality of cis-acting sequences and the importance of
stable transformation to identify tissue-specific
determinants. Spatial information is specified primarily by
two upstream activating sequences (UAS). UAS1 (-295 to -109)
was sufficient for seed-specific expression from both
homologous and heterologous (CaMV 35S) promoters. In situ
localization of GUS expression in tobacco embryos demonstrated
that UAS1 activity was restricted to the cotyledons and shoot
meristem. A second positive domain, UAS2 (-468 to -391),
extended gene activity to the hypocotyl. Temporal control of
GUS expression was found to involve two negative regulatory
sequences, NRS1 (-391 to -295) and NRS2 (-518 to -418), as
well as the positive domain UAS1. The deletion of either
negative element caused premature onset of GUS expression.
These findings indicate combinatorial interactions between
multiple sequence motifs specifying spatial information, and
provide the first example of the involvement of negative
elements in the temporal control of gene expression in higher
plants.
151 NAL Call. No.: 381 J824
Potato tuber type H phosphorylase isoenzyme. Molecular
cloning, nucleotide sequence, and expression of a full-length
cDNA in Escherichia coli. Mori, H.; Tanizawa, K.; Fukui, T.
Baltimore, Md. : American Society for Biochemistry and
Molecular Biology; 1991 Oct05.
The Journal of biological chemistry v. 266 (28): p.
18446-18453; 1991 Oct05. Includes references.
Language: English
Descriptors: Solanum tuberosum; Phosphorylase; Isoenzymes;
Gene expression; Cloning; Dna; Nucleotide sequences; Amino
acid sequences
Abstract: Higher plant tissues contain two alpha-glucan
phosphorylase isozymes (EC 2.4.1.1), types L and H, localized
in the plastid and the cytoplasm, respectively. We already
isolated and sequenced a cDNA clone encoding the type L
isozyme. Presently, a cDNA clone encoding the type H
counterpart was isolated from a cDNA library of immature
potato tuber by plaque hybridization, using two
oligonucleotide probes synthesized based on the partial amino
acid sequences of the type H isozyme. The message encodes a
polypeptide of 838 amino acid residues. Sequence comparison of
the two potato tuber phosphorylase isozymes revealed two major
distinctions; the type L isozyme contains a 78- residue
insertion in the middle of the polypeptide chain as well as a
50-residue amino-terminal extension. Except for these extra
portions, the two isozyme sequences show an identity of 63%.
The entire structural gene for the type H isozyme was inserted
3'-downstream of the strong T7 RNA polymerase promoter in the
expression plasmid pET-3b. Escherichia coli BL21 (DE3) cells
carrying this plasmid produced active phosphorylase upon
induction with isopropyl-beta-D-thiogalactoside at 22 degrees
C. The expression is entirely dependent on the temperature;
the bacteria did not produce a detectable amount of the active
enzyme at 37 degrees C. Addition of pyridoxine to the culture
medium was effective for the enzyme production.
152 NAL Call. No.: QK710.P62
A probable lipid transfer protein gene is induced by NaCl in
stems of tomato plants.
Torres-Schumann, S.; Godoy, J.A.; Pintor-Toro, J.A.
Dordrecht : Kluwer Academic Publishers; 1992 Feb.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(4): p. 749-757; 1992 Feb. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Plant proteins;
Lipid metabolism; Nucleotide sequences; Gene expression;
Messenger RNA; Stems; Genetic regulation; Sodium chloride;
Salinity; Stress; Heat stress; Abscisic acid; Seedlings; Amino
acid sequences
Abstract: A full-length tomato cCDNA clone, TSW12, which is
developmentally and environmentally regulated, has been
isolated and characterized. TSW12 mRNA is accumulated during
tomato seed germination and its level increases after NaCl
treatment or heat shock. In mature plants, TSW12 mRNA is only
detected upon treatment with NaCl, mannitol or ABA and its
expression mainly occurs in stems. The nucleotide sequence of
TSW12 includes an open reading frame coding for a basic
protein of 114 amino acids; the first 23 amino acids exhibit
the sequence characteristic of a signal peptide. The high
similarity between the TSW12-deduced amino acid sequence and
reported lipid transfer proteins suggests that TSW12 encodes a
lipid transfer protein.
153 NAL Call. No.: QH442.B5
Production of active Bacillus licheniformis alpha-amylase in
tobacco and its application in starch liquefaction.
Pen, J.; Molendijk, L.; Quax, W.J.; Sijmons, P.C.; Ooyen,
A.J.J. van; Elzen, P.J.M. van den; Rietveld, K.; Hoekema, A.
New York, N.Y. : Nature Publishing Company; 1992 Mar.
Bio/technology v. 10 (3): p. 292-296; 1992 Mar. Includes
references.
Language: English
Descriptors: Nicotiana tabacum; Bacillus licheniformis;
Transgenics; Genetic transformation; Alpha-amylase; Structural
genes; Gene expression; Seeds; Enzyme activity; Starch;
Hydrolysis; Industrial applications; Starch industry; Food
industry; Potato starch; Maize starch
154 NAL Call. No.: QH442.B5
Production of cyclodextrins, a novel carbohydrate, in the
tubers of transgenic potato plants.
Oakes, J.V.; Shewmaker, C.K.; Stalker, D.M.
New York, N.Y. : Nature Publishing Company; 1991 Oct.
Bio/technology v. 9 (10): p. 982-986; 1991 Oct. Includes
references.
Language: English
Descriptors: Solanum tuberosum; Tubers; Carbohydrates;
Klebsiella; Glycosyltransferases; Genes; Transgenics; Genetic
transformation; Gene expression
155 NAL Call. No.: QK710.P68
A promoter sequence involved in cell-specific expression of
the pea glutamine synthetase GS3A gene in organs of transgenic
tobacco and alfalfa. Brears, T.; Walker, E.L.; Coruzzi, G.M.
Oxford : Blackwell Scientific Publishers and BIOS Scientific
Publishers; 1991 Sep.
The plant journal v. 1 (2): p. 235-244. ill; 1991 Sep.
Includes references.
Language: English
Descriptors: Medicago sativa; Nicotiana; Transgenics; Gene
expression; Gene mapping; Genetic transformation; Nucleotide
sequences; Seed germination; Pisum sativum; Glutamate-ammonia
ligase
156 NAL Call. No.: 81 SO12
Promotive effects of DCPTA on seedling development and growth
of radish. Keithly, J.H.; Yokoyama, H.; Gausman, H.W.
Alexandria, Va. : The Society; 1992 Mar.
Journal of the American Society for Horticultural Science v.
117 (2): p. 294-297; 1992 Mar. Includes references.
Language: English
Descriptors: Raphanus sativus; Seedling growth; Seed
treatment; Growth regulators; Plant development; Growth rate;
Roots; Hypocotyls; Gene expression; Messenger RNA;
Translation; Ribosomes; Crop yield
Abstract: A radish (Raphanus sativus L. cv. Scarlet turnip
white tipped) seedling growth test was examine promotive
effects of
2-(3,4-dichlorophenoxy)triethylamine (DCPTA) on seedling vigor
and plant development. Compared with controls, seed treatment
using 30 micromolar DCPTA significantly (P = 0.05) enhanced
the rates of root and hypocotyl elongation and seedling dry
weight. Enhanced hypocotyl development by DCPTA showed a
significant linear correlation (r = 0.83) with the increased
taproot yield of mature plants grown from DCPTA-treated seeds.
The harvestable taproot yield and harvest index of plants
grown from seeds treated with 30 micromolar DCPTA were
increased 109% and 38%, respectively, as compared with
controls. Incubation of radish seeds in 30 micromolar DCPTA
with actinomycin-D, alpha-amanitin, amiscomycin, or cordycepin
significantly reduced DCTPA-mediated seedling growth. These
results indicate that nuclear gene expression and translation
of mRNA on 80S ribosomes are required for the acceleration of
seedling development by DCPTA.
157 NAL Call. No.: 448.8 V81
Proteolytic maturation of the 206-kDa nonstructural protein
encoded by turnip yellow mosaic virus RNA.
Bransom, K.L.; Weiland, J.J.; Dreher, T.W.
Orlando, Fla. : Academic Press; 1991 Sep.
Virology v. 184 (1): p. 351-357; 1991 Sep. Includes
references.
Language: English
Descriptors: Turnip yellow mosaic tymovirus; Rna; Mutants;
Viral proteins; Proteolysis; Translation; Gene expression
Abstract: The longest open reading frame of turnip yellow
mosaic virus genomic RNA (ORF-206) encodes a 206-kDa
nonstructural protein. The most prominent in vitro translation
products of ORF-206 are the full-length p206 and a shorter N-
coterminal 150-kDa protein. We have confirmed these
assignments by immunoprecipitation of in vitro translation
products with antisera raised to N-terminal and C-terminal
regions encoded by ORF-206. The mechanism by which the 150-kDa
protein arises from ORF-206 was investigated by in vitro
translation of deletion and substitution derivatives
transcribed from pTYMC, a cDNA clone of TYMV RNA. The
following observations demonstrate that the 150-kDa protein
and a C-terminal 70-kDa protein arise from ORF-206 by
autoproteolysis: (1) Two regions encoded by ORF-206 were
necessary for the formation of the 150-kDa protein: a domain
between amino acids 555 and 1051, postulated to encode a
protease, and the region between amino acids 1253 and 1261,
thought to constitute the protease recognition and/or cleavage
site. (2) Mutants with substitutions between amino acids 1253
and 1261 that produce low levels of the 150-kDa protein in in
vitro translations also have high levels of p206 and low
levels of the 70-kDa protein. (3) The rate of formation of the
150-kDa protein is dilution insensitive, suggesting that
proteolysis occurs mainly in cis.
158 NAL Call. No.: 472 N21
Race-specificity of plant resistance to bacterial spot disease
determined by repetitive motifs in a bacterial avirulence
protein.
Herbers, K.; Conrads-Strauch, J.; Bonas, U.
London : Macmillan Magazines Ltd; 1992 Mar12.
Nature v. 356 (6365): p. 172-174; 1992 Mar12. Includes
references.
Language: English
Descriptors: Capsicum annuum; Lycopersicon esculentum;
Xanthomonas campestris pv. vesicatoria; Disease resistance;
Gene expression
Abstract: Elucidation of the genetic and molecular basis of
plant disease resistance is a major objective in the
investigation of plant-microbial interactions. Xanthomonas
campestris pathovar vesicatoria (Xcv), the causal agent of
bacterial spot disease of pepper and tomato, has been
developed as a model host-pathogen system to study the genetic
interactions that specify the expression of plant disease
resistance. Several plant resistance genes (Bs1, Bs2, Bs3)
have been genetically characterized from pepper (Capsicum
annuum) that determine resistance to particular races of the
pathogen carrying specific avirulence genes. For example,
pepper plants carrying the resistance locus Bs3 are resistant
to Xcv strains expressing the avirulence gene avrBs3.
Nucleotide sequence analysis of the avrBs3 gene revealed that
the internal portion of the predicted protein product consists
of a nearly identical 34 amino acid repeat unit, present in
17.5 copies. We report here that the repetitive region of the
avrBs3 gene determines race-specificity and that deletions of
repeat units generate new avirulence specificities and unmask
undiscovered resistance genes in pepper and tomato.
159 NAL Call. No.: 472 N21
Race-specificity of plant resistance to bacterial spot disease
determined by repetitive motifs in a bacterial avirulence
protein.
Herbers, K.; Conrads-Strauch, J.; Bonas, U.
London : Macmillan Magazines Ltd; 1992 Mar12.
Nature v. 356 (6365): p. 172-174; 1992 Mar12. Includes
references.
Language: English
Descriptors: Capsicum annuum; Lycopersicon esculentum;
Xanthomonas campestris pv. vesicatoria; Disease resistance;
Gene expression
Abstract: Elucidation of the genetic and molecular basis of
plant disease resistance is a major objective in the
investigation of plant-microbial interactions. Xanthomonas
campestris pathovar vesicatoria (Xcv), the causal agent of
bacterial spot disease of pepper and tomato, has been
developed as a model host-pathogen system to study the genetic
interactions that specify the expression of plant disease
resistance. Several plant resistance genes (Bs1, Bs2, Bs3)
have been genetically characterized from pepper (Capsicum
annuum) that determine resistance to particular races of the
pathogen carrying specific avirulence genes. For example,
pepper plants carrying the resistance locus Bs3 are resistant
to Xcv strains expressing the avirulence gene avrBs3.
Nucleotide sequence analysis of the avrBs3 gene revealed that
the internal portion of the predicted protein product consists
of a nearly identical 34 amino acid repeat unit, present in
17.5 copies. We report here that the repetitive region of the
avrBs3 gene determines race-specificity and that deletions of
repeat units generate new avirulence specificities and unmask
undiscovered resistance genes in pepper and tomato.
160 NAL Call. No.: 500 N21P
Rapid de novo generation of defective interfering RNA by
cucumber necrosis virus mutants that do not express the 20-kDa
nonstructural protein. Rochon, D.M.
Washington, D.C. : The Academy; 1991 Dec15.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (24): p. 11153-11157. ill; 1991 Dec15.
Includes references.
Language: English
Descriptors: Cucumbers; Necrovirus group; Cloning; Dna; Gene
expression; Mutants; Nucleotide sequences; Rna; Symptoms;
Transcription
Abstract: It is generally believed that serial passage at
high multiplicity of infection (moi) is required for the
generation of defective interfering (DI) particles. High
levels of DI RNAs are found associated with persistent
infections initiated with laboratory cultures of cucumber
necrosis virus (CNV). Two synthetic CNV transcripts that were
derived through site-directed mutagenesis of a highly
infectious CNV cDNA clone and that do not express the CNV 20-
kDa nonstructural protein were found to generate high levels
of symptom-attenuating DI RNAs de novo without serial high-moi
passage in transcript-inoculated plants. Such de novo
generation of DI RNAs did not occur in infections initiated
with wild-type transcript until at least eight serial high-moi
passages. The observation that a CNV nonstructural protein
mutant rapidly generates DI RNA de novo may provide insight
into mechanisms that underly DI particle formation in RNA
viruses in general.
161 NAL Call. No.: 450 P692
Rapid purification and thermostability of the cytoplasmic
aspartate aminotransferase from carrot suspension cultures.
Turano, F.J.; Wilson, B.J.; Matthews, B.F.
Rockville, Md. : American Society of Plant Physiologists; 1991
Oct. Plant physiology v. 97 (2): p. 606-612; 1991 Oct.
Includes references.
Language: English
Descriptors: Daucus carota; Cell suspensions; Cytoplasm;
Purification; Aspartate aminotransferase; Enzyme activity;
Protein analysis; Isoenzymes; Gene expression
Abstract: Several isoenzymic forms of aspartate
aminotransferase (AAT) have been identified in protein
extracts from carrot (Daucus carota) cell suspension cultures.
The cellular location of the major form (form I) of AAT in
carrot suspension cultures was determined by heat
inactivation, subcellular fractionation, and amino acid
sequence analysis. in mammalian systems, there are two forms
of AAT, a heat-stable cytoplasmic form and a heat-labile form
in the mitochondria. The thermostability of three isoenzymes
of carrot AAT was examined, and the results showed that form I
was more thermostable than forms II or III. Organelles were
separated in sucrose gradients by isopynic centrifugation.
Activity for form I was identified in the soluble fractions
and not in fractions containing peroxisomes, proplastids, or
mitochondria. Form I was purified to homogeneity and
endoproteolytically cleaved, and the peptide fragments were
separated by reverse phase chromatography. Analysis of the
sequence data from two of the polypeptides showed that the
amino acid identity of form I is more conserved to the animal
cytoplasmic AAT than to animal mitochondrial AAT sequences.
These data strongly suggest that form I of AAT from carrot is
the cytoplasmic isoenzyme. Additionally, a rapid purification
scheme for form I of AAT from carrot is presented using
selective heat denaturation and anion-exchange chromatography.
162 NAL Call. No.: QK710.P62
Reduced PAL gene suppression in Verticillium-infected
resistant tomatoes. Lee, S.W.; Nazar, R.N.; Powell, D.A.;
Robb, J.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 345-352; 1992 Jan. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Verticillium albo-atrum;
Gene expression; Phenylalanine ammonia-lyase; Genes; Messenger
RNA; Genetic regulation; Pathogenesis; Wilts; Suberin;
Suberization; Xylem; Disease resistance; Defense mechanisms;
Nucleotide sequences; Amino acid sequences
Abstract: In tomato, resistance to the wilt fungus
Verticillium albo-atrum is determined primarily by the Ve
locus. When two tomato near-isolines which differ at this
locus and in their susceptibility to the pathogen were
compared, more rapid suberin coating in the xylem of resistant
plants correlated closely with a more rapid increase in the
activity of phenylalanine ammonia-lyase (PAL; EC 4.3.1.5), an
enzyme which is essential to the suberization process. In
contrast, levels of mRNA did not increase proportionally to
the measured enzyme activities; rather, there was a
substantial suppression of mRNA levels in the susceptible
tomato line, consistent with a much lower elevation of PAL
activity and significantly less vascular coating. The
suppression was absent or substantially reduced in the
resistant line. The results indicate that the pathogen can
suppress defense genes in susceptible plants but suggest that
their expression is altered in resistant hosts and that post-
transcriptional regulation plays a significant role.
163 NAL Call. No.: 450 P692
Regulation of a chitinase gene promoter by ethylene and
elicitors in bean protoplasts.
Roby, D.; Broglie, K.; Gaynor, J.; Broglie, R.
Rockville, Md. : American Society of Plant Physiologists; 1991
Sep. Plant physiology v. 97 (1): p. 433-439; 1991 Sep.
Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Chitinase; Gene expression;
Regulation; Ethylene; Plant pathogens
Abstract: Chitinase gene expression has been shown to be
transcriptionally regulated by a number of inducers, including
ethylene, elicitors, and pathogen attack. To investigate the
mechanism(s) responsible for induction of chitinase gene
expression in response to various stimuli, we have developed a
transient gene expression system in bean (Phaseolus vulgaris)
protoplasts that is responsive to ethylene and elicitor
treatment This system was used to study the expression of a
chimeric gene composed of the 5' flanking sequences of a bean
endochitinase gene fused to the reporter gene beta-
glucuronidase linked to a 3' fragment from nopaline synthase.
Addition of
1-aminocyclopropane-1-carboxylic acid, the direct precursor of
ethylene, or elicitors such as chitin oligosaccharides or cell
wall fragments derived from Colletotrichum lagenarium, to
transformed protoplasts resulted in a rapid and marked
increase in the expression of the chimeric gene. The kinetics
and dose response for these treatments were similar to those
observed for the native gene in vivo. Analyses of 5' deletion
mutants in the protoplast system indicated that DNA sequences
located between -305 and -236 are important for both ethylene
and elicitor induction of the reporter gene.
164 NAL Call. No.: QK710.P62
Regulation of Agrobacterium tumefaciens T-cyt gene expression
in leaves of transgenic potato (Solanum tuberosum L. cv.
Desiree) is strongly influenced by plant culture conditions.
Dymock, D.; Risiott, R.; Pater, S. de; Lancaster, J.; Tillson,
P.; Ooms, G. Dordrecht : Kluwer Academic Publishers; 1991 Oct.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(4): p. 711-725; 1991 Oct. Includes references.
Language: English
Descriptors: Solanum tuberosum; Agrobacterium tumefaciens;
Genetic transformation; Transgenics; Genes; Transferases;
Promoters; Reporter genes; Beta-glucuronidase; Gene
expression; Genetic regulation; Environmental factors; Leaves;
Crown gall; Position effect; In vitro culture; Roots; Stems;
Shoots
Abstract: The promoter region of the Agrobacterium
tumefaciens T-cyt gene was linked in a translational fusion to
the coding DNA of the reporter gene uidA (for beta-
glucuronidase or GUS protein; EC 3.2.1.3 1) and to nos 3'
flanking DNA. The chimaeric gene was introduced by
Agrobacterium transformation into potato (Solanum tuberosum L.
cv. Desiree). In nine transgenic lines, the average GUS levels
were highest in extracts from stems and roots of in vitro
grown plants (ca. 11 000 GUS activity units per pmol MU per mg
protein per min) but lower in leaves of the in vitro grown
plants (ca. 7000 units). GUS activity was intermediate in
stems and roots of plants grown in soil as well as in in vitro
crown galls (ca. 3000 units). Activity was low in tubers,
irrespective of whether these developed in vitro or in soil
(both ca. 100 units), and lowest of all in leaves of soil-
grown plants (ca. 10-15 units). However, in shoot cultures
reestablished from soil-grown plants, GUS activity in the
leaves increased to that determined in the original shoot
cultures. Hence, plant culture conditions strongly influenced
the expression of the T-cyt-uidA-nos gene. In particular, it
was silenced in leaves of soil-grown plants. The results are
compared with previous analyses of the promoter region of the
wild-type T-cyt gene and with the growth properties of a large
number of crown gall cell lines and crown-gall-derived plants,
including over forty S. tuberosum cv. Desiree cell lines
isolated in the present study that were transformed with the
wild-type T-cyt gene and six promoter-mutated derivatives. A
number of implications are discussed for crown gall formation
and for control of expression of plant genes which contain
Activator or G-box type 5' expression control sequences.
165 NAL Call. No.: 450 P692
Regulation of expression of proteinase inhibitor genes by
methyl jasmonate and jasmonic acid.
Farmer, E.E.; Johnson, R.R.; Ryan, C.A.
Rockville, Md. : American Society of Plant Physiologists; 1992
Mar. Plant physiology v. 98 (3): p. 995-1002; 1992 Mar.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Medicago sativa;
Nicotiana tabacum; Proteinases; Enzyme inhibitors; Protein
synthesis; Gene expression; Regulation; Jasmonic acid;
Derivatives; Messenger RNA; Induction
Abstract: Gel electrophoretic analysis of the proteinase
inhibitor proteins induced in tomato leaves by airborne methyl
jasmonate (EE Farmer, CA Ryan [1990] Proc Natl Acad Sci USA
87: 7713-7716) revealed the new appearance of inhibitors I and
II and two other, higher molecular mass proteins (63.5 and 87
kilodaltons). Northern analysis of methyl jasmonate-induced
inhibitors I and II mRNAs in tomato (Lycopersicon esculentum)
leaves, and of alfalfa trypsin inhibitor (a Bowman-Birk family
inhibitor) mRNA in alfalfa (Medicago sativa) leaves, indicated
that nascent inhibitor mRNAs were regulated in a manner
similar to wounding, that is, at the transcriptional level. In
tobacco (Nicotiana tabacum), transformed with a fused gene
composed of the 5' and 3' regions of a wound-inducible potato
inhibitor II and a chloramphenicol acetyl transferase (CAT)
gene coding region, CAT activity was induced in leaves by
methyl jasmonate, consistent with a transcriptional regulation
of the inhibitor II gene. In tomato leaves, inhibitor I and II
mRNAs and proteins accumulated in leaves distal to those
exposed to methyl jasmonate or jasmonic acid to similar levels
as in exposed leaves. We suggest that in response to wound
signals generated by insect or pathogen attacks, linolenic
acid is released into the cytoplasm from plant cell membrane
lipids and is rapidly converted in cells to jasmonic acid (or
perhaps a closely related derivative such as methyl
jasmonate), which serves as a signal to regulate the
expression of proteinase inhibitor genes.
166 NAL Call. No.: TP248.27.P55P52
Regulation of gene expression in ripening tomatoes.
Dellapenna, D.; Giovannoni, J.J.
New York, N.Y. : Chapman and Hall; 1991.
Plant biotechnology v. 2: p. 182-216; 1991. In the series
analytic: Developmental regulation of plant gene expression /
edited by D. Grierson. Literature review. Includes
references.
Language: English
Descriptors: Lycopersicon esculentum; Gene expression; Genetic
regulation; Genes; Fruits; Ripening; Ethylene; Mutants;
Literature reviews
167 NAL Call. No.: 442.8 Z34
Regulation of metallocarboxypeptidase inhibitor gene
expression in tomato. Martineau, B.; McBride, K.E.; Houck,
C.M.
Berlin, W. Ger. : Springer International; 1991 Aug.
M G G : Molecular and general genetics v. 228 (1/2): p.
281-286; 1991 Aug. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Proteinase
inhibitors; Carboxypeptidases; Dna; Cloning; Nucleotide
sequences; Amino acid sequences; Gene expression; Regulation;
Fruits; Gynoecium; Fruiting; Leaves; Abiotic injuries;
Messenger RNA; Genetic regulation; Restriction mapping
Abstract: Tomato fruits contain a metallocarboxypeptidase
inhibitor (MCPI) the sequence of which has already been
determined. Here we report the isolation of a tomato cDNA
clone that encodes the mature MCPI protein as well as an N-
terminal signal peptide for entry into the secretory system
and an eight amino acid carboxy-terminal extension. MCPI RNA
is present at very high levels in anthesis stage ovaries and
decreases quite rapidly during fruit development. MCPI protein
accumulation reflects the pattern of MCPI RNA accumulation in
fruit, consistent with a transcriptional control of MCPI gene
activity. In leaves, the levels of MCPI RNA and protein are
very low. Wounding of the leaves causes a dramatic (100-fold)
increase in steady-state level of MCPI RNA without a
concomitant increase in MCPI protein level suggesting a
control at the post-transcriptional or translational level of
gene expression. Genomic DNA blot hybridization data indicate
that MCPI in tomato may be encoded by a single gene.
168 NAL Call. No.: 448.8 V81
Regulation of the activities of African cassava mosaic virus
promoters by the AC1, AC2, and AC3 gene products.
Haley, A.; Zhan, X.G.; Richardson, K.; Head, K.; Morris, B.
Orlando, Fla. : Academic Press; 1992 Jun.
Virology v. 188 (2): p. 905-909; 1992 Jun. Includes
references.
Language: English
Descriptors: Nicotiana; African cassava mosaic geminivirus;
Dna; Coat proteins; Dna replication; Promoters; Gene
expression; Beta-glucuronidase; Reporter genes; Transgenics;
Protoplasts; Leaves
Abstract: DNA fragments comprising each of the promoter
regions from the geminivirus African cassava mosaic virus
(ACMV) were cloned into the pUC18-based vector, pG1, producing
transcriptional fusions with the beta-glucuronidase gene (GUS)
and nopaline synthase terminator sequence. The relative
activity of each promoter construct was analyzed by a Gus
expression assay of extracts from Nicotiana clevelandii
protoplasts coelectroporated with the GUS reporter constructs
and constructs in which individual ACMV open reading frames
(ORFs) were placed under control of a cauliflower mosaic virus
35S promoter. Results suggest repression of the AC1 gene by
its gene product, which is required for ACMV DNA synthesis.
The promoter activity observed for the single promoter for the
DNA A genes encoding functions of spread and the regulation of
replication (AC2 and AC3 ORFs) was unaffected by
coelectroporation with any of the ACMV ORF constructs.
Promoters for the AV1 (coat protein) gene and the two DNA B
genes (BV1 and BC1) were activated by electroporation of the
AC2 ORF construct. To a lesser extent promoters for the AV1
and BV1 genes were activated with the AC3 ORF construct. The
same pattern of promoter repression and activation was
observed when transgenic N. benthamiana plants expressing the
GUS reporter constructions were inoculated with ACMV DNA A.
169 NAL Call. No.: QK725.P532
Regulation of the osmotin gene promoter.
Kononowicz, A.K.; Nelson, D.E.; Singh, N.K.; Hasegawa, P.M.;
Bressan, R.A. Rockville, Md. : American Society of Plant
Physiologists; 1992 May. The Plant cell v. 4 (5): p. 513-524;
1992 May. Includes references.
Language: English
Descriptors: Nicotiana tabacum; Agrobacterium tumefaciens;
Promoters; Pathogenesis-related proteins; Beta-glucuronidase;
Reporter genes; Enzyme activity; Gene expression; Genetic
regulation; Pollen; Maturation; Pollen germination; Corolla;
Senescence; Fruiting; Sodium chloride; Salinity; Adaptation;
Pericarp; Gynoecium; Roots; Leaves; Epidermis; Mesophyll;
Parenchyma; Xylem; Stems; Histoenzymology; Genetic
transformation; Transgenics
Abstract: By introducing a chimeric gene fusion of the
osmotin promoter and beta-glucuronidase into tobacco by
Agrobacterium-mediated transformation, we have demonstrated a
very specific pattern of temporal and spatial regulation of
the osmotin promoter during normal plant development and after
adaptation to NaCl. We have found that the osmotin promoter
has a very high natural level of activity in mature pollen
grains during anther dehiscence and in pericarp tissue at the
final, desiccating stages of fruit development. GUS activity
was rapidly lost after pollen germination. The osmotin
promoter thus appears to be unique among active pollen
promoters described to date in that it is active only in
dehydrated pollen. The osmotin promoter was also active in
corolla tissue at the onset of senescence. Adaptation of
plants to NaCl highly stimulated osmotin promoter activity in
epidermal and cortex parenchyma cells in the root elongation
zone; in epidermis and xylem parenchyma cells in stem
internodes; and in epidermis, mesophyll, and xylem parenchyma
cells in developed leaves. The spatial and temporal expression
pattern of the osmotin gene appears consistent with both
osmotic and pathogen defense functions of the gene.
170 NAL Call. No.: SB732.6.M65
Resistance to tomato spotted wilt virus infection in
transgenic tobaacco expressing the viral nucleocapsid gene.
MacKenzie, D.J.; Ellis, P.J.
St. Paul, Minn. : APS Press; 1992 Jan.
Molecular plant-microbe interactions : MPMI v. 5 (1): p.
34-40; 1992 Jan. Includes references.
Language: English
Descriptors: Nicotiana tabacum; Transgenics; Plasmids; Genes;
Tomato spotted wilt virus; Genetic transformation; Gene
transfer; Gene expression; Coat proteins; Disease resistance;
Genetic resistance; Induced resistance
171 NAL Call. No.: 448.3 J823
A Rhizobium leguminosarum gene required for symbiotic nitrogen
fixation, melanin synthesis and normal growth on certain
growth media. Hawkins, F.K.L.; Kennedy, C.; Johnston, A.W.B.
Reading : Society for General Microbiology; 1991 Jul.
The Journal of general microbiology v. 137 (pt.7): p.
1721-1728; 1991 Jul. Includes references.
Language: English
Descriptors: Pisum; Rhizobium leguminosarum; Azotobacter
vinelandii; Escherichia coli; Nitrogen fixation; Genes;
Melanins; Biosynthesis; Growth; Plasmids; Mutations; Mutants;
Gene expression; Nitrates; Succinic acid; Nutrient sources;
Nodules
Abstract: The gene nfrX in Azotobacter vinelandii activates
transcription of other nif genes in that species. A cosmid
containing cloned Rhizobium leguminosarum DNA that corrected
the Nif- defect of an nfrX mutant of A. vinelandii was
isolated. Following Tn5 transposon mutagenesis of the cosmid
in Escherichia coli, mutant derivatives unable to correct the
A. vinelandii nfrX mutants were obtained in two separate
regions of DNA. In addition, mutations close to one of the
nfrX regions conferred a complex phenotype when introduced
into the Rhizobium genome by marker exchange. These mutants
induced non-fixing nodules on peas, were slow-growing on media
with succinate as C source or nitrate as N source and, when
present in R. leguminosarum biovar phaseoli, they failed to
make melanin, a pigment that is normally synthesized by R. l.
bv. phaseoli. The mutated gene, termed melC, was fused to uidA
(which encodes beta-glucuronidase); it was found that
transcription of melC-uidA was enhanced in microaerobic
conditions and that it was expressed at high levels in
infection threads in pea nodules.
172 NAL Call. No.: 450 P692
Rhizobium nod gene inducers exuded naturally from roots of
common bean (Phaseolus vulgaris L.).
Hungria, M.; Joseph, C.M.; Phillips, D.A.
Rockville, Md. : American Society of Plant Physiologists; 1991
Oct. Plant physiology v. 97 (2): p. 759-764; 1991 Oct.
Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Root exudates; Plant
composition; Flavonoids; Transcription; Induction; Rhizobium
leguminosarum; Gene expression; Nodulation
Abstract: Four compounds exuded from young roots of a black-
seeded bean (Phaseolus vulgaris L., cv PI165426CS) induce
transcription of nod genes in Rhizobium leguminosarum biovar
phaseoli. The three most active nod gene inducers were
identified by spectroscopic methods (ultraviolet/visible
absorbance, proton nuclear magnetic resonance, and mass
spectrometry) as being eriodictyol (5,7,3',4'-
tetrahydroxyflavanone), naringenin (5,7,4'-
trihydroxyflavanone), and a 7-O-glycoside of genistein
(5,7,4'-trihydroxyisoflavone). Comparisons with authentic
standards verified the chemical structures of the aglycones
and their capacity to induce beta-galactosidase activity in R.
leguminosarum strains containing nodA-lacZ or nodC-lacZ
fusions controlled by R. leguminosarum biovar phaseoli nodD
genes. Roots of 9-day-old seedlings released 42, 281, and 337
nanomoles per plant per day of genistein, eriodictyol, and
naringenin, respectively. Genistein and naringenin induced
higher maximum beta-galactosidase activities and required
lower concentrations for half-maximum induction than
eriodictyol. Comparing the nod gene-inducing activity of seed
rinses with root exudate from PI165426CS bean showed that root
flavonoids were released at about 6% the rate of those from
seeds on a molar basis, but on average the individual
compounds from roots were approximately three times more
active than nod gene inducers from seeds.
173 NAL Call. No.: QH506.E46
Ribosomal frameshifting in plants: a novel signal directs the
-1 frameshift in the synthesis of the putative viral replicase
of potato leafroll luteovirus. Prufer, D.; Tacke, E.; Schmitz,
J.; Kull, B.; Kaufmann, A.; Rohde, W. Oxford, Eng. : IRL
Press; 1992 Mar.
The EMBO journal - European Molecular Biology Organization v.
11 (3): p. 1111-1117; 1992 Mar. Includes references.
Language: English
Descriptors: Potato leaf roll luteovirus; Genomes; Rna; Rna
polymerase; Genes; Translation; Genetic code; Ribosomes; Gene
expression; Viral proteins; Molecular conformation
Abstract: The 5.8 kb RNA genome of potato leafroll luteovirus
(PLRV) contains two overlapping open reading frames, ORF2a and
ORF2b, which are characterized by helicase and RNA polymerase
motifs, respectively, and possibly represent the viral
replicase. Within the overlap, ORF2b lacks an AUG
translational start codon and is therefore presumably
translated by -1 ribosomal frameshifting as a transframe
protein with ORF2a. This hypothesis was studied by introducing
the putative frameshift region into an internal position of
the beta-glucuronidase (GUS) gene and testing for the
occurrence of frameshifting in vivo by transient expression of
GUS activity in potato protoplasts as well as in vitro by
translation in the reticulocyte system. Both experimental
approaches demonstrate that a -1 frameshift occurs at a
frequency of approximately 1%. Site-directed mutagenesis
identified the frameshift region and the involvement of the
novel heptanucleotide motif UUUAAAU in conjunction with an
adjacent stem-loop structure. Part of this stem-loop encodes a
basic region in the ORF2b moiety of the transframe protein
which was shown by binding experiments with PLRV RNA to
represent a nucleic acid-binding domain. These data support a
possible biological significance of the frameshift to occur at
this position of the large overlap by including the putative
RNA template-binding site of the PLRV replicase in the
ORF2a/ORF2b transframe protein.
174 NAL Call. No.: 450 P692
Ripening-related gene from avocado fruit--ethylene-inducible
expression of the mRNA and polypeptide.
McGarvey, D.J.; Sirevag, R.; Christoffersen, R.E.
Rockville, Md. : American Society of Plant Physiologists; 1992
Feb. Plant physiology v. 98 (2): p. 554-559; 1992 Feb.
Includes references.
Language: English
Descriptors: Persea Americana; Fruits; Ripening; Genetic
regulation; Gene expression; Messenger RNA; Polypeptides;
Protein composition; Ethylene
Abstract: Fruit ripening involves a series of changes in gene
expression regulated by the phytohormone ethylene. AVOe3, a
ripening-related gene in avocado fruit (Persea americana Mill.
cv Hass), was characterized with regard to its ethylene-
regulated expression. The AVOe3 mRNA and immunopositive
protein were induced in mature fruit within 12 hours of
propylene treatment. The AVOe3 mRNA levels reached a maximum 1
to 2 days before the ethylene climacteric, whereas the
immunopositive protein continued to accumulate. RNA selected
by the pAVOe3 cDNA clone encoded a polypeptide with molecular
mass of 34 kilodaltons, corresponding to the molecular mass of
the AVOe3 protein determined by immunoblots. The protein was
soluble, remaining in solution at 100,000 gravity and eluted
as a monomer on gel filtration. Because of its pattern of
induction and relationship to an ethylene-related gene of
tomato, the possible involvement of AVOe3 in ethylene
biosynthesis is discussed.
175 NAL Call. No.: 442.8 Z34
RNA-protein interactions at transcript 3' ends and evidence
for trnK-psbA cotranscription in mustard chloroplasts.
Nickelsen, J.; Link, G.
Berlin, W. Ger. : Springer International; 1991 Aug.
M G G : Molecular and general genetics v. 228 (1/2): p. 89-96;
1991 Aug. Includes references.
Language: English
Descriptors: Sinapis alba; Messenger RNA; Binding site;
Binding proteins; Nucleotide sequences; Gene expression;
Transcription; Genes; Molecular mapping; Ribonucleases; Enzyme
activity; Chloroplasts; Chloroplast genetics; Deletions
Abstract: In vitro transcripts from the 3' flanking regions
of mustard chloroplast genes were tested for protein binding
in a chloroplast extract. Efficient and sequence-specific RNA-
protein interaction was detected with transcripts of the genes
trnK, rps16 and trnH, but not with the 3' terminal region of
trnQ RNA. The transacting component required for specific
complex formation is probably a single 54 kda polypeptide. The
protein-binding region of the rps16 3' terminal region was
mapped and compared with that of the trnK transcript
determined previously. Both regions reveal a conserved 7-mer
UUUAUCU followed by a stretch of U residues. Deletion of the
trnK 3' U cluster resulted in more than 80% reduction in the
binding activity, and after deletion of both the U stretch and
the 7-mer motif no binding at all was detectable. RNase
protection experiments indicate that the protein-binding
regions of both the rps16 and trnK transcripts correlate with
the positions of in vivo 3' ends, suggesting an essential role
for the 54 kDa binding protein in RNA 3' end formation. In the
case of the trnK gene, evidence was obtained for read-through
transcripts that extend into the psbA coding region, thus
pointing to the possibility of trnK-psbA cotranscription.
176 NAL Call. No.: QH426.C8
The role of coxI-associated repeated sequences in plant
mitochondrial DNA rearrangements and radish cytoplasmic male
sterility.
Makaroff, C.A.; Apel, I.J.; Palmer, J.D.
Berlin, W. Ger. : Springer International; 1991.
Current genetics v. 19 (3): p. 183-190; 1991. Includes
references.
Language: English
Descriptors: Raphanus sativus; Mitochondrial genetics;
Cytoplasmic male sterility; Mitochondrial DNA; Cytochrome-c
oxidase; Multigene families; Repetitive DNA; Nucleotide
sequences; Amino acid sequences; Recombination; Loci;
Transcription; Gene expression; Messenger RNA; Restriction
mapping
Abstract: The gene coxI, encoding subunit I of mitochondrial
cytochrome c oxidase, has been characterized from the normal
(fertile) and Ogura (male-sterile) cytoplasms of radish to
determine if a previously identified mitochondrial DNA
rearrangement, and its associated transcriptional differences,
could play a role in Ogura cytoplasmic male sterility (CMS).
The normal and Ogura loci are virtually identical for 2.8 kb.
including a 527-codon open reading frame whose product is
approximately 95% identical to other plant COXI polypeptides.
A rearrangement 120 bp 5' to the coding region results in
different 5' transcript termini for the two genes. A
comparison of several crucifer mitochondrial DNAs indicates
that this rearrangement also occurs in the normal radish
cytoplasm and is, therefore, not involved in Ogura CMS.
Sequences present at the coxI locus belong to at least two
different dispersed repeat families, members of which are also
associated with other rearranged genes in radish.
177 NAL Call. No.: QK710.P62
Salt-inducible betaine aldehyde dehydrogenase from sugar beet:
cDNA cloning and expression.
McCue, K.F.; Hanson, A.D.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(1): p. 1-11; 1992 Jan. Includes references.
Language: English
Descriptors: Beta vulgaris; Multiple genes; Oxidoreductases;
Cloning; Nucleotide sequences; Amino acid sequences; Gene
expression; Messenger RNA; Salinity; Salt tolerance; Osmotic
pressure; Stress; Betaine
Abstract: Members of the Chenopodiaceae, such as sugar beet
and spinach, accumulate glycine betaine in response to
salinity or drought stress. The last enzyme in the glycine
betaine biosynthetic pathway is betaine aldehyde dehydrogenase
(BADH). In sugar beet the activity of BADH was found to
increase two- to four-fold in both leaves and roots as the
NaCl level in the irrigation solution was raised from 0 to 500
millimoles. This increase in BADH activity was paralleled by
an increase in level of translatable BADH mRNA. Several cDNAs
encoding BADH were cloned from a lambdagt10 library
representing poly(A)+ RNA from salinized leaves of sugar beet
plants, by hybridization with a spinach BADH cDNA. Three
nearly full-length cDNA clones were confirmed to encode BADH
by their nucleotide and deduced amino acid sequence identity
to spinach BADH; these clones showed minor nucleotide sequence
differences consistent with their being of two different BADH
alleles. The clones averaged 1.7 kb and contained an open
reading frame predicting a polypeptide of 500 amino acids with
83% identity to spinach BADH. RNA gel blot analysis of total
RNA showed that salinization to 500 mM NaCl increased BADH
mRNA levels four-fold in leaves and three-fold in the taproot.
DNA gel blot analyses indicated the presence of at least two
copies of BADH in the haploid sugar beet genome.
178 NAL Call. No.: 442.8 Z34
Sequence variability and gene structure at the self-
incompatibility locus of Solanum tuberosum.
Kaufmann, H.
M G G : Molecular and general genetics. p. 457-466. Includes
references.
Language: English
Abstract: Allelic complexity is a key feature of self-
incompatibility (S) loci in gametophytic plants. We describe
in this report the allelic diversity and gene structure of the
S locus in Solanum tuberosum revealed by the isolation and
characterization of genomic and cDNA clones encoding S-
associated major pistil proteins from three alleles (S1, Sr1,
S2). Genomic clones encoding the S1 and S2 proteins provide
evidence for a simple gene structure: Two exons are separated
by a small intron of 113 (S1) and 117 bp (S2). Protein
sequences deduced from cDNA clones encoding S1 and Sr1
proteins show 95% homology. 15 of the 25 residues that differ
between these S1 and Sr1 alleles are clustered in a short
hypervariable protein segment (amino acid positions 44-68),
which corresponds in the genomic clones to DNA sequences
flanking the single intron. In contrast, these alleles are
only 66% homologous to the S2 allele, with the residues that
differ between the alleles being scattered throughout the
sequence, DNA crosshybridization experiments identify a
minimum of three classes of potato S alleles: one c<<
00802729oct92 P352: PRINT S38/0/ALL TAP
179 NAL Call. No.: 500 N21P
A short C-terminal sequence is necessary and sufficient for
the targeting of chitinases to the plant vacuole.
Neuhaus, J.M.; Sticher, L.; Meins, F. Jr; Boller, T.
Washington, D.C. : The Academy; 1991 Nov15.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (22): p. 10362-10366; 1991 Nov15.
Includes references.
Language: English
Descriptors: Cucumis sativus; Nicotiana sylvestris; Nicotiana
tabacum; Plant secretions; Vacuoles; Amino acid sequences;
Chitinase; Defense mechanisms; Disease resistance; Enzyme
activity; Fungal diseases; Gene expression; Polypeptides
Abstract: Tobacco contains different isoforms of chitinase
(EC 3.2.1.14), a hydrolase thought to be involved in the
defense against pathogens. Deduced amino acid sequences for
putatively vacuolar, basic chitinases differ from the
homologous extracellular, acidic isoforms by the presence of a
C-terminal extension. To examine the role of this C-terminal
extension in protein sorting, Nicotiana silvestris plants were
stably transformed with chimeric genes coding for tobacco
basic chitinase A with and without the seven C-terminal amino
acids. In plants expressing unmodified chitinase A, the enzyme
activity was low in the intercellular wash fluid but high in
protoplasts and isolated vacuoles. In contrast, in plants
expressing mutant chitinase lacking the C terminus, the
activity was high in the intercellular wash fluid but low in
protoplasts. N. silvestris plants were also transformed with
similar constructions coding for a structurally unrelated,
extracellular cucumber chitinase. In plants expressing
unmodified cucumber chitinase, its activity was present in the
intercellular wash fluid and absent from protoplasts. In
plants expressing cucumber chitinase with the C-terminal
extension from tobacco chitinase A, activity was low in
intercellular wash fluids but high in protoplasts and
vacuoles. These results demonstrate that the C-terminal
extension of tobacco chitinase A is necessary and sufficient
for the vacuolar localization of chitinases and, therefore,
that it comprises a targeting signal for plant vacuoles.
180 NAL Call. No.: QK710.P62
Spatial and temporal expression patterns directed by the
Agrobacterium tumefaciens T-DNA gene 5 promoter during somatic
embryogenesis in carrot. Mattsson, J.; Borkird, C.; Engstrom,
P.
Dordrecht : Kluwer Academic Publishers; 1992 Feb.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(4): p. 629-637; 1992 Feb. Includes references.
Language: English
Descriptors: Daucus carota; Agrobacterium tumefaciens; Gene
expression; Reporter genes; Beta-glucuronidase; Promoters;
Recombinant DNA; Dna; Somatic embryogenesis; Temporal
variation; Spatial variation; Plant embryos; Cotyledons;
Hypocotyls; Radicles; Shoots; Roots; Genetic transformation;
Transgenics
Abstract: We have analysed the patterns of expression of a
gene encoding beta-glucuronidase (GUS) fused to the promoter
of the Agrobacterium tumefaciens T-DNA gene 5 during
embryogenesis in carrot, Daucus carota L. Gene expression was
monitored by a histochemical assay of beta-glucuronidase
activity. The gene 5 promoter, although of bacterial origin,
conferred expression upon the marker gene in all stages of
embryo development. The patterns of expression however,
differed between embryos in different stages of development.
In the globular stage expression was confined to the basal
part of the embryo, suggesting that the promoter is sensitive
to regulatory functions active in the primary establishment of
polarity in the radially symmetric globular embryo. In the
heart and torpedo stages of development GUS expression was
high in the entire embryonic axis, but not in the cotyledons.
During germination expression was reduced in the elongating
hypocotyl and radicle, and high levels of expression were
detected only in the shoot and root apices. Among the
transformed cell lines analysed, one was found that showed an
aberrant pattern of GUS expression during embryogenesis, in
that expression in the upper part of the embryo was
undetectable, and expression was restricted to the root apex
in later stages of development. This difference in organ
specificity of expression is likely due to a large deletion of
the promoter.
181 NAL Call. No.: 500 N21P
A steroid-inducible gene expression system for plant cells.
Schena, M.; Lloyd, A.M.; Davis, R.W.
Washington, D.C. : The Academy; 1991 Dec01.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (23): p. 10421-10425. ill; 1991 Dec01.
Includes references.
Language: English
Descriptors: Arabidopsis thaliana; Chemoreceptors; Dna
sequencing; Gene expression; Glucocorticoids; Nucleotide
sequences; Steroids
Abstract: Promoters that allow the selective induction of
gene expression in vivo constitute an important methodology in
eukaryotic organisms such as yeast and the fruit fly, but to
date no such system has been described for higher plants.
Given the fact that mammalian steroid receptors can function
as hormone-dependent inducers of gene expression in
heterologous systems, the feasibility of using mammalian
steroid hormones as selective inducers of plant gene
expression was investigated. Here it is shown that the
glucocorticoid receptor expressed in plant cells is capable of
activating a test gene linked to glucocorticoid response
elements, providing the transfected plant cells are treated
with glucocorticoid hormone. Nanomolar concentrations of
glucocorticoids are sufficient to induce gene expression more
than 150-fold, without causing detectable alterations in the
physiology of the cultured plant cells. These findings
indicate that glucocorticoid induction of steroid-responsive
promoters should provide a general method for regulating gene
expression in plant cells and imply that such a system might
ultimately function in whole plants such as Arabidopsis
thaliana.
182 NAL Call. No.: QK710.P62
Strong negative and positive regulatory elements contribute to
the high-level fruit-specific expression of the tomato 2A11
gene.
Haaren, M.J.J. van; Houck, C.M.
Dordrecht : Kluwer Academic Publishers; 1991 Oct.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(4): p. 615-630; 1991 Oct. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Promoters;
Controlling elements; Gene expression; Messenger RNA; Fruits;
Fruiting; Transgenics; Reporter genes; Beta-glucuronidase;
Histoenzymology
Abstract: Fruit-specific expression of beta-glucuronidase
(GUS) activity was produced in transgenic tomato plants when
the GUS-coding region was flanked by 5' and 3' regions of the
tomato 2A11 gene. Deletion studies on the 5' region revealed a
number of strong regulatory elements involved in the proper
expression of the 2A11 gene. A 4.0 kb and a 1.3 kb 5' region
can confer high-level fruit-specific GUS expression, while a
1.8 kb 5' region produces no GUS activity in leaf or fruit
tissue. Thus, a strong negative regulatory element is present
in the region between 1324 bp and 1796 bp upstream of the 2A11
transcriptional start and a strong fruit-specific positive
regulatory element is present more than 1.8 kb upstream of the
transcriptional start site. The 1.8 kb promoter region can be
activated by the upstream insertion of the CaMV 35S enhancer
sequence, albeit not in a fruit-specific fashion. Substitution
of the 3' region of the 2A11 gene with a different 3' region
does not seem to affect GUS expression significantly,
indicating a minor role, if any, for the 3' region in the
fruit-specific expression of the 2A11 gene.
183 NAL Call. No.: 381 J824
Structural comparison, modes of expression, and putative cis-
acting elements of the two 4-coumarate:CoA ligase genes in
potato.
Becker-Andre, M.; Schulze-Lefert, P.; Hahlbrock, K.
Baltimore, Md. : American Society for Biochemistry and
Molecular Biology; 1991 May05.
The Journal of biological chemistry v. 266 (13): p. 8551-8559;
1991 May05. Includes references.
Language: English
Descriptors: Solanum tuberosum; Coumaric acids; Coenzyme a;
Ligases; Gene expression; Cloning; Nucleotide sequences; Amino
acid sequences
Abstract: 4-Coumarate:CoA ligase (4CL), a key enzyme of
phenylpropanoid metabolism in plants, is encoded in potato
(Solanum tuberosum L.) by two structurally similar genes
(St4cl-1, St4cl-2). Computer-based sequence analyses revealed
similarities at the amino acid sequence level with other
enzymes dependent on ATP for activation of aromatic carboxylic
acids, e.g. some bacterial peptide synthetases. All these
enzymes have a common seven amino acid sequence motif
containing one cysteine residue. Using an assay on the basis
of the polymerase chain reaction, we show that the mRNAs from
both 4CL genes accumulate to equal levels in suspension-
cultured cells and whole plant tissues, independent of various
kinds of activating stimulus applied and of the overall
transcriptional activity of the genes. The apparent lack of
differential expression, together with the fact that both 4CL
genes and proteins are nearly identical in structure, make it
unlikely that 4CL isoforms in potato have specific roles in
metabolic channeling. Constitutive in vivo footprints in the
TATA-box proximal region of the St4cl-1 promoter define
putative cis-acting elements which may be involved in the
responses of the 4CL genes to various endogenous and exogenous
stimuli.
184 NAL Call. No.: 442.8 Z34
Structure and expression of AtS1, an Arabidopsis thaliana gene
homologous to the S-locus related genes of Brassica.
Dwyer, K.G.; Lalonde, B.A.; Nasrallah, J.B.; Nasrallah, M.E.
Berlin, W. Ger. : Springer International; 1992 Feb.
M G G : Molecular and general genetics v. 231 (3): p. 442-448;
1992 Feb. Includes references.
Language: English
Descriptors: Arabidopsis thaliana; Brassica oleracea;
Multigene families; Glycoproteins; Self incompatibility;
Nucleotide sequences; Amino acid sequences; Restriction
mapping; Gene expression; Messenger RNA; Buds; Flowers
Abstract: Genetic and molecular analysis of the self-
incompatibility locus (S-locus) of the crucifer Brassica has
led to the characterization of a multigene family involved in
pollen-stigma interactions. While the crucifer Arabidopsis
thaliana does not have a self-incompatibility system, S-
related sequences were detected in this species by cross-
hybridization with Brassica DNA probes. In this paper, we show
that an A. thaliana S-related sequence, designated AtS1, is
expressed specifically in flower buds. Sequence analysis
suggests that AtS1 encodes a secreted glycoprotein that is
most similar to the Brassica S-locus related protein SLR1. As
has been proposed for SLR1, this gene may be involved in
determining some fundamental aspect of pollen-stigma
interactions during pollination. The molecular and genetic
advantages of the Arabidopsis system will provide many avenues
for testing this hypothesis.
185 NAL Call. No.: 385 J822
Structure and regulated expression of Kunitz chymotrypsin
inhibitor genes in winged bean [Psophocarpus tetragonolobus
(L.) DC.].
Habu, Y.; Peyachoknagul, S.; Umemoto, K.; Sakata, Y.; Ohno, T.
Tokyo : Japanese Biochemical Society; 1992 Feb.
Journal of biochemistry v. 111 (2): p. 249-258; 1992 Feb.
Includes references.
Language: English
Descriptors: Psophocarpus tetragonolobus; Chymotrypsin
inhibitors; Structural genes; Gene expression; Genetic
regulation; Nucleotide sequences; Amino acid sequences
Abstract: We analyzed the structure and the expression of
Kunitz chymotrypsin inhibitor (WCI) genes in winged bean. WCI
was encoded by a multigene family which comprised at least
seven members. From their primary structures, four genes
(WCI-2, WCI-3a, WCI-3b, and WCI-x) were expected to be
functional ones and the other three (WCI-P1, WCI-P2, and WCI-
P3) to be pseudogenes. The nucleotide sequences of the WCI-3a
and WCI-3b genes were nearly identical, and they encoded the
WCI-3 protein, the major chymotrypsin inhibitor in seeds. The
WCI-2 gene also encoded the chymotrypsin inhibitor found in
seeds and the WCI-x gene was expected to encode an
unidentified chymotrypsin inhibitor. WCI messenger RNA and
protein accumulated mainly in developing seeds and tuberous
roots, small amounts of WCI mRNA being present in stems and
pericarps. In seeds, transient accumulation of WCI mRNA was
observed during the seed maturation period. These results
suggest that the expression of WCI genes is regulated organ-
specifically and developmentally in winged bean.
186 NAL Call. No.: QK710.P62
Sugar response element enhances wound response of potato
proteinase inhibitor II promoter in transgenic tobacco.
Kim, S.R.; Costa, M.A.; An, G.
Dordrecht : Kluwer Academic Publishers; 1991 Nov.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(5): p. 973-983; 1991 Nov. Includes references.
Language: English
Descriptors: Solanum tuberosum; Nicotiana tabacum;
Agrobacterium tumefaciens; Genetic transformation;
Transgenics; Proteinase inhibitors; Promoters; Reporter genes;
Chloramphenicol acetyltransferase; Gene expression; Abiotic
injuries; Genetic regulation; Sugars; Sucrose; Controlling
elements; Deletions; Molecular mapping; Nucleotide sequences
Abstract: The promoter region of the potato proteinase
inhibitor II (PI-II) gene was studied to identify cis-acting
regulatory sequences involved in sugar response using
transgenic tobacco plants. The 5' control region covering an
892 nucleotide sequence upstream from the cap site and a 32
nucleotide untranslated region of the PI-II promoter was able
to activate a reporter chloramphenicol acetyltransferase (cat)
gene by wounding or by incubating in a sugar-free medium. This
wound response was further enhanced by sugar. Hexoses,
disaccharides, and some trisaccharides were strong inducers
whereas pentoses, deoxy sugars, sugar acids, TCA cycle
intermediates, amino acids, and other carbohydrates had little
effect on the promoter activity. Deletion of the sequence
between -892 and -573 abolished the wound response but not the
sugar response. An additional 5' deletion to -453 removed the
sugar inducibility. Locations of the cis-acting regulatory
elements were further elucidated by 3' deletion analysis.
Deletion of the downstream region from -520 did not affect the
wound or sugar response of the promoter. However, 3' deletion
mutant -574 was unable to respond to sugar but did respond
weakly to wounding. Further deletion to -624 abolished both
responses. Therefore, it can be concluded that a wound
response element is located in between -624 and -574 and that
the response is further enhanced by a sugar response element
located in the sequence between -573 and -520.
187 NAL Call. No.: 450 P692
Sugar-dependent expression of the CHS-A gene for chalcone
synthase from petunia in transgenic Arabidopsis.
Tsukaya, H.; Ohshima, T.; Naito, S.; Chino, M.; Komeda, Y.
Rockville, Md. : American Society of Plant Physiologists; 1991
Dec. Plant physiology v. 97 (4): p. 1414-1421; 1991 Dec.
Includes references.
Language: English
Descriptors: Petunia; Arabidopsis thaliana; Transgenics; Gene
transfer; Gene expression; Naringenin-chalcone synthase;
Enzyme activity; Genetic regulation; Sugars; Hybrids;
Nucleotide sequences
Abstract: Transgenic Arabidopsis thaliana plants were
constructed by introduction of a fusion of the gene for beta-
glucuronidase (GUS) to the CHS-A gene, which is one of the two
genes for chalcone synthase that are actively expressed in the
floral organs of petunia. The expression of the fusion gene
CHS-A::GUS was low in transgenic Arabidopsis plantlets, but it
was enhanced when plantlets or detached leaves were
transferred to a medium that contained 0.3 molar sucrose,
glucose, or fructose. No enhancement was observed when
plantlets were transferred to a medium that contained 0.3
molar mannitol. Measurements of cellular levels of sugars
revealed a tight linkage between the level of expression of
the CHS-A::GUS gene and the level of accumulation of
exogenously supplied sugars, in particular sucrose. The
parallelism between the organ-specific accumulation of sugar
and the organ-specific expression of the CHS-A::GUS gene was
also observed in petunia and A. thaliana plants grown under
normal conditions in soil. The consensus sequences for sugar
responses, such as boxes II and III in members of the family
of sporamin genes from the sweet potato, were found in the
promoter region of the CHS-A gene that was used for fusion to
the GUS gene. It is suggested that the expression of the CHS-A
gene is regulated by sugars, as is the expression of other
sugar-responsive genes, such as the genes for sporamin. A
putative common mechanism for the control of expression of
"sugar-related" genes, including the CHS-A gene, is discussed.
188 NAL Call. No.: QK710.P62
Suppression of gene expression in plant cells utilizing
antisense sequences transcribed by RNA polymerase III.
Bourque, J.E.; Folk, W.R.
Dordrecht : Kluwer Academic Publishers; 1992 Jul.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(4): p. 641-647; 1992 Jul. Includes references.
Language: English
Descriptors: Glycine max; Daucus carota; Antisense DNA;
Recombinant DNA; Transfer RNA; Methionine; Reporter genes;
Chloramphenicol acetyltransferase; Regulation; Gene
expression; Rna polymerase; Enzyme activity; Transcription;
Rna
Abstract: Inverted sequences of the chloramphenicol
acetyltransferase (CAT) reporter gene were fused to a soybean
tRNA(met(i)) gene lacking a terminator such that the
tRNA(met(i)) sequences caused the co-transcription of CAT
antisense sequences by RNA polymerase III. When electroporated
into carrot protoplasts, these antisense DNA constructs
suppressed CAT enzyme activity expressed from co-
electroporated DNAs containing the CAT gene downstream of the
cauliflower mosaic virus (CaMV) 35S RNA promoter. Our most
effective construct, an antisense sequence complementary to
the 3' portion of the CAT gene, inhibited CAT activity five-
fold greater than an antisense construct expressed by RNA
polymerase II from the cauliflower mosaic virus 35S RNA
promoter. These results indicate that antisense sequences
transcribed by RNA polymerase III should efficiently suppress
gene expression in plants.
189 NAL Call. No.: QK710.P62
Survey of plastid RNA abundance during tomato fruit ripening:
the amounts of RNA from the ORF 2280 region increase in
chromoplasts.
Richards, C.M.; Hinman, S.B.; Boyer, C.D.; Hardison, R.C.
Dordrecht : Kluwer Academic Publishers; 1991 Dec.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(6): p. 1179-1188; 1991 Dec. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Dna; Genomes;
Chloroplasts; Plastids; Gene expression; Messenger RNA; Rna;
Fruits; Ripening; Ripening stage; Restriction mapping;
Nucleotide sequences; Amino acid sequences; Chloroplast
genetics
Abstract: A comprehensive survey of the levels of plastid
RNAs at progressive stages of tomato fruit ripening was
conducted by hybridizing total RNA with labeled Pst I
fragments that cover almost the entire tomato plastid genome
and with gene-specific probes. Two different cultivars of
tomato (Lycopersicon esculentum Mill.) were examined, Traveler
76 and Count II. One of the tomato probes, P7, revealed a
pronounced increase in the amount of an 8.3 kb RNA in ripe
fruit. The homologous region of the tobacco plastid genome
contains several genes for ribosomal proteins and a large
unidentified open reading frame (2280 codons). Little change
was observed in the levels of many transcripts during
ripening. However, in some cases (e.g. psbA and psbC/D) the
amount of RNA decreased during ripening of Count II but showed
little or no change in Traveler 76. The contrast between
Traveler 76 and Count II tomatoes shows that the level of
plastid transcripts can vary substantially during fruit
ripening with no obvious effect on the chloroplast to
chromoplast transition. The large RNA from the P7 region may
encode a protein that functions predominantly in chromoplasts.
190 NAL Call. No.: QK710.A9
Synthesis of spinach phosphoribulokinase and ribulose 1,5-
bisphosphate in Escherichia coli.
Hudson, G.S.; Morell, M.K.; Arvidsson, Y.B.C.; Andrews, T.J.
East Melbourne : Commonwealth Scientific and Industrial
Research Organization; 1992.
Australian journal of plant physiology v. 19 (3): p. 213-221;
1992. Includes references.
Language: English
Descriptors: Spinacia oleracea; Escherichia coli; Ribulose
1,5-diphosphate; Kinases; Biosynthesis; Dna; Gene transfer;
Gene expression; Targeted mutagenesis; Mutants; Plasmids;
Genetic regulation
191 NAL Call. No.: SB599.P45
Temperature and genotype interactions in the expression of
host resistance in lettuce downy mildew.
Judelson, H.S.; Michelmore, R.W.
London : Academic Press; 1992 Apr.
Physiological and molecular plant pathology v. 40 (4): p.
233-245; 1992 Apr. Includes references.
Language: English
Descriptors: Lactuca sativa; Bremia lactucae; Host
specificity; Disease resistance; Genotypes; Gene expression;
Virulence; Genes; Environmental factors; Air temperature;
Genotype environment interaction
Abstract: The influence of temperature and genotype on
infection types determined by 13 gene-for-gene interactions
between lettuce and the downy mildew fungus, Bremia lactucae,
was evaluated. Lettuce seedlings containing each of 13
resistance (Dm) genes were inoculated with isolates of B.
lactucae expressing various combinations of the matching
avirulence genes, and incubated at 5, 10, 15, or 22 degrees C.
Resistance, assessed by the absence of sporulation, became
less effective at lower temperatures for Dm6, Dm7, Dm11, Dm15,
and Dm16. No change was observed for resistance conditioned by
eight other gene-for-gene interactions. Histological
examination indicated that the extent of fungal development in
host tissue was dependent on the interacting genotypes and on
temperature. Manipulation of interactions involving Dm7 and
Dm11, using temperature-shift incubation regimes, indicated
that continued and cumulative exposure to permissive
temperatures was required for effective resistance and
suggested that the determinants of specificity are present in
most host cells and are expressed throughout fungal
development.
192 NAL Call. No.: QK710.P62
Temperature treatments of dark-grown pea seedlings cause an
accelerated greening in the light at different levels of gene
expression. Otto, B.; Ohad, I.; Kloppstech, K.
Dordrecht : Kluwer Academic Publishers; 1992 Mar.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(5): p. 887-896; 1992 Mar. Includes references.
Language: English
Descriptors: Pisum sativum; Gene expression; Messenger RNA;
Air temperature; Heat shock; Greening; Light; Morphogenesis;
Circadian rhythm; Thylakoids; Chloroplasts; Plant proteins;
Xanthophylls; Plasma membranes
Abstract: We have previously shown that heat-shock in the
dark evokes photomorphogenesis-like effects and circadian
rhythmicity at the level of mRNAs when applied to emerging pea
plantlets during several consecutive days [15]. Here we extend
these findings by showing that a temperature shift to 10
degrees C above average and a single heat-shock are sufficient
for induction of circadian rhythmicity and changes in
morphogenesis. The maximum response to a single heat-shock
occurs at days 2 to 3 after sowing indicating additional
developmental control of the response. An increasing number of
heat-shock treatments intensifies the morphogenetic effect.
The heat-shocked plantlets have an elevated level of the
xanthophyll lutein in the dark. Upon illumination of heat-
shocked plantlets accumulation of chloroplast pigments as well
as that of individual thylakoid membrane proteins and their
corresponding mRNAs occur much faster than in the etiolated
controls. This is reflected in an accelerated formation of
grana stacks. Therefore, heat-shock seems to evoke a
responsiveness of plantlets similar to that obtained earlier
by other authors using pre-illumination. The working
hypothesis is put forward that induction or synchronization of
circadian rhythmicity by either light or heat-shock might be
sufficient to explain the observed morphogenetic changes.
193 NAL Call. No.: QP501.E8
Tissue distribution and change in potato starch phosphorylase
mRNA levels in wounded tissue and sprouting tubers.
Bhatt, A.M.; Knowler, J.T.
New York, NY : Springer-Verlag New York Inc; 1992 Mar.
European journal of biochemistry v. 204 (3): p. 971-975; 1992
Mar. Includes references.
Language: English
Descriptors: Solanum tuberosum; Starch; Phosphorylase;
Messenger RNA; Gene expression; Clones; Tuber sprouting;
Injuries; Tubers; Stems; Stolons; Roots; Leaves
Abstract: Starch phosphorylase has been cloned from a lambda
gt10 cDNA library of potato tuber mRNA. Selected recombinants
have been used to demonstrate that phosphorylase mRNA is most
abundant in tubers but is also detectable in stolon, root,
stem and leaf tissue. The level of phosphorylase mRNA was
greatly reduced in wounded stem and tuber tissue. The
wounding-induced decrease in phosphorylase mRNA levels is not
reversed in the presence of sucrose or mannitol. Regional
differences are described in the levels of phosphorylase and
patatin mRNA in different parts of the tuber and in the shoot
of sprouting potatoes.
194 NAL Call. No.: QK725.P532
The tomato 66.3-kD polyphenoloxidase gene: molecular
identification and developmental expression.
Shahar, T.; Hennig, N.; Gutfinger, T.; Hareven, D.; Lifschitz,
E. Rockville, Md. : American Society of Plant Physiologists;
1992 Feb. The Plant cell v. 4 (2): p. 135-147; 1992 Feb.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Genes; Catechol oxidase;
Nucleotide sequences; Restriction mapping; Amino acid
sequences; Apical meristems; Flowers; Messenger RNA; Gene
expression; Copper; Binding site; Leaves; Flowering; Mutants
Abstract: A gene coding for a polypeptide abundant in tomato
floral meristems was isolated and shown to represent a tomato
66.3-kD polyphenoloxidase. Analysis of cDNA clones and a
corresponding intronless genomic clone indicated that the
plastid-bound 587-residue-long polypeptide, designated P2,
contains two conserved copper-binding domains, similar to
those found in fungal and mammalian tyrosinases. P2
transcripts and polypeptides are accumulated in the arrested
floral primordia of the ananths mutant inflorescences and are
equally abundant in primordia of wild-type flowers; the gene
continues to be expressed at high levels in developing floral
organs. in young expanding leaves, P2 protein is concentrated
in palisade cells and in epidermal trichomes. Expression
patterns of P2 in plant meristems permit molecular distinction
between floral and vegetative primordia, and, in a companion
study, comparison with dUTPase suggests that the two genes
mark two alternative complementary developmental programs in
the floral and vegetative meristems of the tomato plants.
195 NAL Call. No.: QK710.P62
The tomato Cu,Zn superoxide dismutase genes are
developmentally regulated and respond to light and stress.
Perl-Treves, R.; Galun, E.
Dordrecht : Kluwer Academic Publishers; 1991 Oct.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(4): p. 745-760; 1991 Oct. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Gene expression;
Superoxide dismutase; Copper; Zinc; Genes; Genetic regulation;
Light; Paraquat; Abiotic injuries; Drought; Ethylene;
Ethephon; Stress; Transcription; Translation; Messenger RNA;
Enzyme activity
Abstract: The expression of the two Cu, Zn superoxide
dismutase (SOD) genes of tomato was followed in different
organs and plant developmental stages at the transcript and
enzymatic activity levels. The cDNA clones used as probes code
for the chloroplast Cu Zn SOD (clone T1) and the cytosolic Cu
Zn SOD (clone P31). The two genes were found to display
distinct expression patterns. While the T1 transcript was rare
or absent from roots, stems and ripening fruits, the P31
transcript was very abundant in these organs. Shoot tips,
flower buds, seedlings and young leaves contained high levels
of the two mRNAs. During leaf expansion, the levels of both
transcripts diminish markedly. Despite the diminished presence
of transcripts, SOD activity levels of the corresponding
cytosolic and chloroplast isozymes accumulated and were
sustained throughout leaf expansion. In non-photosynthetic
organs, the SOD-3 (cytosolic) isozyme contained most of the
activity, while in the expanded leaf the SOD-1 (chloroplast)
isozyme was more abundant. Light-regulated accumulation of
both the P31 transcript (1.7-fold) and the T1 transcript (3-
fold) was observed upon light exposure of etiolated seedlings.
However, only SOD-1 activity was observed to increase, after a
lag of a few hours. The levels of both transcripts increased
in response to paraquat and mechanical wounding. The level of
the cytosolic transcript and the respective isozyme activity
increased dramatically during prolonged drought stress while
the chloroplast transcript remained unaffected. The expression
of both genes was enhanced by spraying tomato plants with
ethephon--a compound that releases ethylene. Our data show
that the expression of Cu Zn SOD genes in tomato is modulated
in response to a variety of factors and suggest the importance
of oxyradical toxicity as well as the role of SOD in the
defence mechanism of plants exposed to stress.
196 NAL Call. No.: 381 J824
A tomato gene expressed during fruit ripening encodes an
enzyme of the carotenoid biosynthesis pathway.
Bartley, G.E.; Viitanen, P.V.; Bacot, K.O.; Scolnik, P.A.
Baltimore, Md. : American Society for Biochemistry and
Molecular Biology; 1992 Mar15.
The Journal of biological chemistry v. 267 (8): p. 5036-5039;
1992 Mar15. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Carotenoids;
Biosynthesis; Biochemical pathways; Enzymes; Structural genes;
Gene expression; Ripening; Nucleotide sequences; Amino acid
sequences
Abstract: In the initial stages of carotenoid biosynthesis in
plants the enzyme phytoene synthase converts two molecules of
geranylgeranyl diphosphate into phytoene, the first carotenoid
of the pathway. We show here that a tomato (Lycopersicon
esculentum) cDNA for a gene (Psy1) expressed during fruit
ripening directs the in vitro synthesis of a 47-kDa protein
which, upon import into isolated chloroplasts, is processed to
a mature 42-kDa form. The imported protein is largely
associated with membranes, but it can be easily solubilized by
dilution or by treatment at high pH. A plasmid construct
containing prokaryotic promoter and ribosome-binding sequences
fused to the Psyl cDNA complements the carotenoidless
phenotype of a Rhodobacter capsulatus crtB mutant. We conclude
that Psy1 encodes phytoene synthase and that this enzyme is a
peripheral plastid membrane protein.
197 NAL Call. No.: QK710.P62
The tomato nia gene complements a Nicotiana plumbaginifolia
nitrate reductase-deficient mutant and is properly regulated.
Dorbe, M.F.; Caboche, M.; Daniel-Vedele, F.
Dordrecht : Kluwer Academic Publishers; 1992 Jan.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(2): p. 363-375; 1992 Jan. Includes references.
Language: English
Descriptors: Nicotiana plumbaginifolia; Lycopersicon
esculentum; Genetic transformation; Transgenics; Nitrate
reductase; Genes; Complementation; Mutants; Gene expression;
Transcription; Genetic regulation; Light; Nitrate; Enzyme
activity; Messenger RNA
Abstract: A nitrate reductase (NR) deficient mutant of
Nicotiana plumbaginifolia totally impaired in the production
of functional nia transcript and protein was restored for NR
activity by transformation with a cloned tomato nia gene. The
transgenic plants expressed from undetectable to 17% of the
control NR activity in their leaves. Restoration of growth
rates comparable to the wild type was obtained for transgenic
plants expressing as little as 10% of the wild-type activity
showing that nitrate reduction is not a growth-limiting factor
in the wild-type plant. The analysis of the transgene
expression showed that the tomato nia gene transcription was
regulated by light, nitrate and a circadian rhythm as in
tomato plants. These results suggest that all the cis-acting
sequences involved in these regulations are contained in the 3
kb upstream region of the tomato nia gene and are still
functional in transgenic N. plumbaginifolia plants. The amount
of NR transcript synthesized from the tomato nia gene was
reduced when a functional N. plumbaginifolia nia locus was
introduced by sexual crosses. These data support the
hypothesis that nitrate reduction is regulated by nitrate-
derived metabolites as demonstrated in fungi.
198 NAL Call. No.: QK710.P62
Transcriptional regulation of a seed-specific carrot gene,
DC8. Goupil, P.; Hatzopoulos, P.; Franz, G.; Hempel, F.D.;
You, R.; Sung, Z.R. Dordrecht : Kluwer Academic Publishers;
1992 Apr.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 18
(6): p. 1049-1063; 1992 Apr. Includes references.
Language: English
Descriptors: Daucus carota; Transcription; Gene expression;
Genes; Promoters; Genetic regulation; Abscisic acid; Seeds;
Plant embryos; Protoplasts; Embryogenesis; Callus;
Transgenics; Genetic transformation; Reporter genes; Beta-
glucuronidase; Dna binding proteins; Controlling elements
Abstract: Many late embryogenesis abundant (Lea) protein
genes in plants are regulated by abscisic acid (ABA). The RNA
level of a carrot gene, DC8, increases in response to ABA in
developing seeds. However, DC8 cannot be induced by ABA in
adult tissues. We used chimeric genes made of various DC8
promoter fragments fused to beta-glucuronidase (GUS) to
analyze the transcriptional regulation of DC8. DC8:GUS
expression was measured in electroporated carrot protoplasts
and in stably transformed carrots. The region of the DC8
promoter from -170 to -51 contained ABA-responsive sequences
that required a 5' upstream region for high levels of
expression in embryogenic callus protoplasts. 505 bp of the
DC8 promoter conferred GUS expression in stably transformed
somatic and zygotic embryos. DC8:GUS was expressed only in
tissues formed in the seed. This includes cells in the embryo,
the endosperm and the germinating seedlings. Gel retardation
and competition experiments were performed to analyze the
embryo nuclear protein-DNA binding activities in vitro. No
binding activity was detected on the putative ABA-responsive
region; however the 5' upstream regions located between -505
and -301 interacted with embryo nuclear factors. An additional
site of DNA-protein interaction was located between positions
-32 and +178. The nuclear proteins that bind these sequences
were found in the embryo nuclei only, not in the nuclei from
leaves or roots.
199 NAL Call. No.: QK710.P62
Transformation of cauliflower (Brassica oleracea L. var.
botrytis)-- and experimental survey.
Eimert, K.; Siegemund, F.
Dordrecht : Kluwer Academic Publishers; 1992 Jun.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 19
(3): p. 485-490; 1992 Jun. Includes references.
Language: English
Descriptors: Brassica oleracea var. botrytis; Agrobacterium
tumefaciens; Genetic transformation; Direct DNAuptake;
Electroporation; Gene transfer; Gene expression; Reporter
genes; Phosphotransferases; Protoplasts; Leaves
Abstract: The paper compares different approaches for the
genetic transformation of cauliflower (Agrobacterium-mediated,
PEG-mediated and/or electroporation). Transient expression of
the neomycin phosphotransferase II (NPTII) gene could be
detected after direct gene transfer. Stable transformation was
achieved using both Agrobacterium-mediated and direct gene
transfer. Expression as well as incorporation of the NPTII
sequence could be demonstrated.
200 NAL Call. No.: SD13.C35
Transgenic Populus hybrid expresses a wound-inducible potato
proteinase inhibitor II--CAT gene fusion.
Klopfenstein, N.B.; Shi, N.Q.; Kernan, A.; McNabb, H.S. Jr;
Hall, R.B.; Hart, E.R.; Thornburg, R.W.
Ottawa, Ont. : National Research Council of Canada; 1991 Sep.
Canadian journal of forest research; Journal canadien de
recherche forestiere v. 21 (9): p. 1321-1328; 1991 Sep.
Includes references.
Language: English
Descriptors: Populus alba; Populus grandidentata; Hybrids;
Genetic transformation; Agrobacterium tumefaciens;
Transgenics; Genetic markers; Genes; Gene expression;
Chimeras; Enzyme inhibitors; Proteinases
Abstract: A hybrid poplar clone has been transformed with a
previously constructed wound-inducible potato proteinase
inhibitor (pin2) -chloramphenicol acetyltransferase (CAT)
chimeric gene linked to a nopaline synthase (nos)-neomycin
phosphotransferase II (NPT II) selectable marker gene. The
Populus alba X Populus grandidentata Hansen clone was
transformed by means of leaf cocultivation with Agrobacterium
tumefaciens strain A281 containing a binary vector. Shoots
were regenerated and rooted on selective medium containing
kanamycin sulfate. Subsequently, plants were established in
soil for greenhouse and field growth. NPT II activity from the
nos-NPT Il selectable marker gene was observed in leaf
extracts, thereby confirming expression of the transferred
selectable marker gene in poplar. Southern hybridization
confirmed the incorporation of a single copy of the pin2-CAT
construction into the genome of the transformed hybrid
poplars. Northern analysis of transgenic poplar leaves
demonstrated that the potato pin2-CAT gene construction also
was inducible in this woody dicotyledon. Thus, the wound-
inducible promoter from an herbaceous dicot functions in a
distinct family of woody dicots.
201 NAL Call. No.: 511 P444AEB
Transgenic potato plants containing a foreign potato X virus
coat protein gene.
Glagotskaya, T.Ts; Shul'ga, O.A.; Sidorov, V.A.; Zakhar'ev,
V.M.; Skryabin, K.G.; Gleba, Yu.Yu
New York, N.Y. : Consultants Bureau; 1991 Mar.
Doklady : biological sciences - Akademiia nauk SSSR v. 314
(1/6): p. 605-607. ill; 1991 Mar. Translated from: Doklady
Akademii Nauk SSSR, v. 314 (5), 1990, p. 1240-1242. (511
P444A). Includes references.
Language: English; Russian
Descriptors: Solanum tuberosum; Transgenics; Cultivars;
Disease resistance; Potato x potexvirus; Transcription; Gene
expression; Coat proteins
202 NAL Call. No.: QK725.P54
Transient expression in electroporated pea protoplasts:
elicitor responsiveness of a phenylalanine ammonia-lyase
promoter. Hashimoto, T.; Yamada, T.; Tada, A.; Kawamata, S.;
Tanaka, Y.; Sriprasertsak, P.; Ichinose, Y.; Kato, H.; Izutsu,
S.; Shiraishi, T.
Berlin, W. Ger. : Springer International; 1992 May.
Plant cell reports v. 11 (4): p. 183-187. ill; 1992 May.
Includes references.
Language: English
Descriptors: Pisum sativum; Protoplasts; Callus; Cell
suspensions; Chloramphenicol acetyltransferase; Gene
expression; Phenylalanine ammonia-lyase; Promoters; Enzyme
activity; Nucleotide sequences
Abstract: High yields of viable pea protoplasts were produced
from suspension cultured cells and the conditions for the
optimum transient expression of the chloramphenicol
acetyltransferase (CAT) gene fused to the CaMV 35S promoter
after electroporation were investigated. Conditions for
elicitor induction of a member of the phenylalanine ammonia-
lyase (PAL) gene family in pea was also investigated using a
chimeric gene carrying 480 bp of the putative promoter region
of gPAL1 connected to bacterial cat gene and nos terminator.
CAT activity was considerably induced by the treatment with
fungal elicitor (> 100 micrograms/ml glucose equivalent)
isolated from Mycosphaerella pinodes, a pea pathogen.
203 NAL Call. No.: QK710.P62
Transient expression of beta-glucuronidase in Arabidopsis
thaliana leaves and roots and Brassica napus stems using a
pneumatic particle gun. Seki, M.; Komeda, Y.; Iida, A.;
Yamada, Y.; Morikawa, H.
Dordrecht : Kluwer Academic Publishers; 1991 Aug.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(2): p. 259-263; 1991 Aug. Includes references.
Language: English
Descriptors: Arabidopsis thaliana; Brassica napus; Genetic
transformation; Direct DNAuptake; Gene transfer; Laboratory
equipment; Gene expression; Reporter genes; Beta-
glucuronidase; Roots; Stems; Leaves; Histoenzymology
Abstract: Successful transient expression of beta-
glucuronidase (GUS) in Arabidopsis thaliana leaves and roots
and Brassica napus stems was obtained after gene delivery with
a pneumatic particle gun driven by compressed air. Effects of
the pneumatic pressure used to accelerate the particles
(accelerating pressure; 85 to 200 kg/cm2) and of preculture
periods of plant tissues (0 to 6 days) on the efficiency of
gene delivery were studied. In A. thaliana leaves, best
results were obtained at 115 kg/cm2 of accelerating pressure
and 3 days of preculture. In A. thaliana roots, the optimum
was at 200 kg/cm2 of accelerating pressure and 3 days of
preculture. These results indicate that both preculture period
and accelerating pressure are vital factors that determine the
efficiency of gene delivery by particle gun.
204 NAL Call. No.: QK710.P63
Transient gene expression in electroporated bean cotyledon
protoplasts. Bustos, M.M.; Battraw, M.J.; Kalkan, F.A.; Hall,
T.C.
Athens, Ga. : International Society for Plant Molecular
Biology, University of Georgia; 1991 Nov.
Plant molecular biology reporter - ISPMB v. 9 (4): p. 322-332;
1991 Nov. Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Gene transfer; Gene
expression; Cotyledons; Protoplasts; Laboratory methods
205 NAL Call. No.: QK725.P54
Transient gene expression in strawberry (Fragaria X ananassa
Duch.) protoplasts and the recovery of transgenic plants.
Nyman, M.; Wallin, A.
Berlin, W. Ger. : Springer International; 1992.
Plant cell reports v. 11 (2): p. 105-108; 1992. Includes
references.
Language: English
Descriptors: Fragaria ananassa; Protoplasts; Gene transfer;
Transgenics; Gene expression; Beta-glucuronidase; Enzyme
activity; Callus; Regenerative ability; Genetic transformation
Abstract: A transient beta-glucuronidase (GUS)-assay was
performed to evaluate electroporation parameters and optimize
DNA delivery conditions into strawberry protoplasts. Optimal
GUS-activity was obtained when protoplasts were subjected to
400 V/cm for 20 ms. GUS-activity could be further increased by
the addition of carrier DNA to the electroporation mixture.
Callus selected on 10 microgram/ml hygromycin produced shoots
which exhibited GUS-activity. The transformed nature of the
shoots obtained after selection was confirmed by DNA-analysis.
206 NAL Call. No.: QK710.P62
Trasient gene expression in cassava using high-velocity
microprojectiles. Franche, C.; Bogusz, D.; Schopke, C.;
Fauquet, C.; Beachy, R.N. Dordrecht : Kluwer Academic
Publishers; 1991 Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 493-498; 1991 Sep. Includes references.
Language: English
Descriptors: Manihot esculenta; Arabidopsis thaliana; Genetic
transformation; Direct DNAuptake; Beta-glucuronidase;
Reporter genes; Promoters; Gene expression; Leaves;
Transgenics
Abstract: The bacterial gene encoding beta-glucuronidase
(GUS) was transiently expressed in cassava leaves following
the introduction of the gene by microparticle bombardment. The
DNA expression vector used to introduce the reporter gene is a
pUC 19 derivative and consisted of a CaMV 35S promoter (P35S),
the GUS coding region and 7S polyadenylation region. Several
other promoters and regulating sequences were tested for
efficiency in cassava leaves. Two derivatives of the P35S, one
including a partial duplication of the upstream region of the
P35S and the other containing a tetramer of the octopine
synthase enhancer, were found to be expressed at three times
the level of the P35S in cassava leaves. The ubiquitin 1
promoter from Arabidopsis thaliana was expressed at the same
level as the P35S. No influence on the level of expression was
observed when different 3' ends were used. The biolistic
transient gene expression system in cassava leaves allows
rapid analysis of gene constructs and can serve as a
preliminary screen for chimeric gene function in the
construction of transgenic cassava plants.
207 NAL Call. No.: 448.8 V81
Turnip crinkle virus genes required for RNA replication and
virus movement. Hacker, D.L.; Petty, I.T.D.; Wei, N.; Morris,
T.J.
Orlando, Fla. : Academic Press; 1992 Jan.
Virology v. 186 (1): p. 1-8; 1992 Jan. Includes references.
Language: English
Descriptors: Brassica campestris; Chenopodium amaranticolor;
Nicotiana; Protoplasts; Turnip crinkle carmovirus; Rna; Coat
proteins; Genes; Clones; Mutants; Replication; Movement; Gene
expression; Nucleotide sequences
Abstract: We have used infectious in vitro transcripts from
mutagenized turnip crinkle virus (TCV) cDNA clones to identify
the gene products required for viral RNA replication, virion
assembly, and intercellular movement. Previous sequence
analysis of the TCV genome revealed the presence of five open
reading frames which had the potential to encode gene products
of 88, 38, 28, 9, and 8 kDa. Inoculation of protoplasts with
infectious RNA revealed that only the p28 and p88 gene
products are required for viral RNA synthesis. Although the p8
and p9 gene products were dispensable for RNA replication and
virion assembly in protoplasts, mutations in the p8 and p9
genes prevented the production of systemic infections in
plants. No viral RNA or protein was observed in the inoculated
or systemic leaves of plants inoculated with transcripts
synthesized from p8 or p9 mutant cDNAs. in contrast to these
results, viral RNA was recovered from the inoculated, but not
the systemic leaves, of plants inoculated with an RNA lacking
the coat protein (CP) gene. With the CP mutant, no symptoms
were observed on normally systemic hosts, but small local
lesions were induced on Chenopodium amaranticolor. These
results indicate that p8, p9, and CP are required for viral
movement.
208 NAL Call. No.: QK725.P532
Two anthranilate synthase genes in Arabidopsis: defense-
related regulation of the tryptophan pathway.
Niyogi, K.K.; Fink, G.R.
Rockville, Md. : American Society of Plant Physiologists; 1992
Jun. The Plant cell v. 4 (6): p. 721-733; 1992 Jun. Includes
references.
Language: English
Descriptors: Arabidopsis thaliana; Multiple genes; Structural
genes; Oxo-acid-lyases; Nucleotide sequences; Amino acid
sequences; Restriction mapping; Exons; Chromosome maps; Gene
expression; Genetic regulation; Defense mechanisms; Abiotic
injuries; Pseudomonas syringae pv. tomato; Pseudomonas
syringae pv. maculicola; Messenger RNA
Abstract: Arabidopsis thaliana has two genes, ASA1 and ASA2,
encoding the alpha subunit of anthranilate synthase, the
enzyme catalyzing the first reaction in the tryptophan
biosynthetic pathway. As a branchpoint enzyme in aromatic
amino acid biosynthesis, anthranilate synthase has an
important regulatory role. The sequences of the plant genes
are homologous to their microbial counterparts. Both predicted
proteins have putative chloroplast transit peptides at their
amino termini and conserved amino acids involved in feedback
inhibition by tryptophan. ASA1 and ASA2 cDNAs complement
anthranilate synthase alpha subunit mutations in the yeast
Saccharomyces cerevisiae and in Escherichia coli, confirming
that both genes encode functional anthranilate synthase
proteins. The distributions of ASA1 and ASA2 mRNAs in various
parts of Arabidopsis plants are overlapping but nonidentical,
and ASA1 mRNA is approximately 10 times more abundant in whole
plants. Whereas ASA2 is expressed at a constitutive basal
level, ASA1 is induced by wounding and bacterial pathogen
infiltration, suggesting a novel role for ASA1 in the
production of tryptophan pathway metabolites as part of an
Arabidopsis defense response. Regulation of key steps in
aromatic amino acid biosynthesis in Arabidopsis appears to
involve differential expression of duplicated genes.
209 NAL Call. No.: 500 N21P
Two genes encoding 1-aminocyclopropane-1-carboxylate synthase
in zucchini (Cucurbita pepo) are clustered and similar but
differentially regulated. Huang, P.L.; Parks, J.E.; Rottmann,
W.H.; Theologis, A.
Washington, D.C. : The Academy; 1991 Aug15.
Proceedings of the National Academy of Sciences of the United
States of America v. 88 (16): p. 7021-7025; 1991 Aug15.
Includes references.
Language: English
Descriptors: Cucurbita pepo; Amino acid sequences; Cloning;
Cycloheximide; Ethylene; Gene expression; Genetic code;
Lyases; Nucleotide sequences; Transcription
Abstract: A 17-kilobase (kb) region of the zucchini
(Cucurbita pepo) genome has been sequenced and contains two
genes, CP-ACC1A and CP-ACC1B, encoding 1-aminocyclopropane-1-
carboxylate synthase (ACC synthase; S-adenosyl-L-methionine
methylthioadenosine-lyase, EC 4.4.1.14). The genes are
transcribed convergently and are separated by a 5.7-kb
intergenic region. Their coding regions are interrupted by
four introns located in identical positions. While the DNA
identity in their coding regions is 97%, their 5' and 3'
flanking regions are highly divergent. Transcription of CP-
ACC1A is rapidly induced by wounding in fruit and etiolated
hypocotyls and by indoleacetic acid (IAA)/benzyladenine/Lici
only in fruit tissue. Conditions that induce CP-ACC1B
expression have not been found. Protein synthesis inhibition
derepresses the expression of CP-ACC1A and other unidentified
ACC synthase genes, suggesting that they may be under negative
control. The amine acid sequences deduced from the nucleotide
sequences of the genes are 493 and 494 residues long with 95%
identity. The most notable feature of the amino acid sequence
is the presence of 11 of the 12 invariant amino acid residues
involved in the binding of the substrate and pyridoxal-5'-
phosphate in various aminotransferases. We conclude that ACC
synthase is encoded by a multigene family of which certain
members are differentially induced by auxin in a tissue-
specific manner. Furthermore, ACC synthase, a pyridoxal-
containing enzyme, may have an
evolutionaryrelationship with the superfamily of
aminotransferases.
210 NAL Call. No.: 450 P692
Uniquely regulated proteinase inhibitor I gene in a wild
tomato species: Inhibitor I family gene is wound-inducible in
leaves and developmentally regulated in fruit.
Wingate, V.P.M.; Ryan, C.A.
Rockville, Md. : American Society of Plant Physiologists; 1991
Oct. Plant physiology v. 97 (2): p. 496-501; 1991 Oct.
Includes references.
Language: English
Descriptors: Lycopersicon peruvianum; Fruits; Protein
analysis; Proteinases; Enzyme inhibitors; Genetic regulation;
Gene expression; Restriction mapping; Nucleotide sequences
Abstract: A uniquely regulated proteinase inhibitor I gene
was isolated from the wild tomato species Lycopersicon
peruvianum (L.) Mill. (LA107) and characterized. The inhibitor
gene is wound-inducible in leaves and is expressed in unripe
fruit during development. The gene (lambda clone 1) is present
on a 15.5 kilobase pair Sal1-SalI genomic DNA fragment.
Southern blot analysis of L. peruvianum genomic DNA shows only
one strongly hybridizing DNA fragment to probes derived from X
clone 1. S1 nuclease protection experiments and Northern
analyses confirm that this gene is both wound-inducible in
leaves and developmentally regulated in young unripe fruit.
These observations are supported by comparisons of the 5'-
flanking DNA sequences of the L. peruvianum inhibitor I gene
with known elicitor responsive cis-acting sequences. The
transcriptional regulation of the lambda clone 1 inhibitor I
gene in leaves of wounded plants and in developing unripe
fruit indicates that the gene contains unique complex
regulating elements. These elements respond to both
environmental and developmental tissue-specific signals that
can regulate proteinase inhibitor synthesis to protect the
tissues of this wild species of tomato against predators and
pathogens.
211 NAL Call. No.: QK725.P532
Vascular-specific expression of the bean GRP 1.8 gene in
negatively regulated. Keller, B.; Baumgartner, C.
Rockville, Md. : American Society of Plant Physiologists; 1991
Oct. The Plant cell v. 3 (10): p. 1051-1061; 1991 Oct.
Includes references.
Language: English
Descriptors: Phaseolus vulgaris; Nicotiana tabacum; Genetic
regulation; Gene expression; Plant proteins; Cell wall
components; Vascular system; Stems; Deletions; Genes;
Promoters; Reporter genes; Beta-glucuronidase;
Histoenzymology; Transgenics; Genetic transformation;
Chimeras; Controlling elements
Abstract: In French bean, the glycine-rich cell wall protein
GRP 1.8 is specifically synthesized in the vascular tissue. To
identity cis-acting sequences required for cell type-specific
synthesis of GRP 1.8, expression patterns of fusion gene
constructs were analyzed in transgenic tobacco. In these
constructs, the uidA (beta-glucuronidase) gene was placed
under control of 5' upstream deletions as well as internal
deletions of the GRP 1.8 promoter. Four different cis-acting
regulatory regions, SE1 and SE2 (stem elements), a negative
regulatory element, and a root-specific element, were found to
control the tissue-specific expression. Deletion of the
negative regulatory element resulted in expression of the uidA
gene in cell types other than vascular cells. The SE1 region
was essential for expression in several cell types in the
absence of further upstream regulatory sequences. Full-length
promoters having insertions between the negative regulatory
element and SE1 strongly expressed the gene in nonvascular
cell types in stems and leaves. Thus, vascular-specific
expression of the GRP 1.8 promoter is controlled by a complex
set of positive and negative interactions between cis-acting
regulatory regions. The disturbance of these interactions
results in expression in additional cell types.
212 NAL Call. No.: 450 P692
Wild-type levels of abscisic acid are not required for heat
shock protein accumulation in tomato.
Bray, E.A.
Rockville, Md. : American Society of Plant Physiologists; 1991
Oct. Plant physiology v. 97 (2): p. 817-820; 1991 Oct.
Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Protein synthesis; Heat
shock proteins; Regulation; Abscisic acid; Heat tolerance;
Genotypes; Genetic variation; Gene expression
Abstract: Levels of endogenous abscisic acid (ABA) in wild
type were not required for the synthesis of heat shock
proteins in detached leaves of tomato (Lycopersicon esculentum
Mill., cv Ailsa Craig). Heat-induced alterations in gene
expression were the same in the ABA-deficient mutant of
tomato, flacca, and the wild type. Heat tolerance of the
mutant was marginally less that the wild type, and in
contrast, ABA applications significantly reduced the heat
tolerance of wild-type leaves. It was concluded that elevated
levels of endogenous ABA are not involved in the tomato heat
shock response.
213 NAL Call. No.: 450 J8224
Wound response in mechanically isolated asparagus mesophyll
cells: a model monocotyledon system.
Harikrishna, K.; Paul, E.; Darby, R.; Draper, J.
Oxford : Oxford University Press; 1991 Jun.
Journal of experimental botany v. 42 (239): p. 791-799; 1991
Jun. Includes references.
Language: English
Descriptors: Asparagus officinalis; Abiotic injuries;
Mechanical damage; Mesophyll; Cell suspensions; Cell division;
Cell differentiation; Respiration; Gene expression; Messenger
RNA; Transcription; Dna replication; Ribosomal RNA; Ribosomal
DNA; Plant proteins; Cytology
Abstract: Cells at a wound surface in large organ explants
are normally very difficult to study at the molecular level.
We describe the use of mechanically isolated Asparagus
mesophyll cell suspensions as alternative explants in which
the majority of the cells are viable, damaged in a uniform
manner and available in large numbers. Asparagus cells respond
to wounding and to the culture medium by rapid cell expansion
on day 3 post-isolation which precedes cell division by 24 h.
Cell expansion was accompanied by a large rise in respiration
rate and a massive increase in RNA synthesis; DNA content had
only doubled by day 4. SDS-PAGE analysis of proteins showed
that several polypeptides were absent, or present at a lower
abundance, in 3-6-d-old wounded cells. Conversely, several
novel polypeptides had appeared by this time which were not
present in unwounded cladode; in particular, a large band at
16 kD was noted. Two dimensional PAGE analysis of protein
translated in vitro using poly (A)+ mRNA isolated from
asparagus cells harvested at different times after wounding
demonstrated that there was a major qualitative change in the
message population and that much of the alteration in gene
expression was probably controlled at the level of
transcription. We believe that mechanically isolated asparagus
cells provide a useful model system for the study of wound-
induced cellular dedifferentiation and for the generation of
wound-enriched mRNA populations.
214 NAL Call. No.: QK710.P62
Wound-regulated accumulation of specific transcripts in tomato
fruit: interactions with fruit development, ethylene and
light.
Parsons, B.L.; Mattoo, A.K.
Dordrecht : Kluwer Academic Publishers; 1991 Sep.
Plant molecular biology : an international journal on
molecular biology, biochemistry and genetic engineering v. 17
(3): p. 453-464; 1991 Sep. Includes references.
Language: English
Descriptors: Lycopersicon esculentum; Gene expression;
Messenger RNA; Cloning; Dna; Nucleotide sequences; Abiotic
injuries; Genetic regulation; Ripening; Ethylene; Light;
Ripening stage; Fruits
Abstract: Regulation of three cDNA clones (pT52, pT53, and
pT58) was analyzed in terms of wounding alone and wounding in
conjunction with developmental and environmental cues
(ripening, ethylene, and light) in tomato fruit tissue. The
pT52-specific transcript level is induced by wounding in
early-red and red stage fruit and by ethylene. The pT58-
specific transcript level is also induced by wounding and
ethylene in early-red stage fruit but is not induced by
wounding in red fruit. The pT53-specific transcript level is
repressed by wounding in early-red and red stage fruit. Like
the pT52- and pT58-specific transcripts, the pT53-specific
transcript is induced by ethylene. Furthermore, the level of
the pT52-specific transcript is regulated by light. Analysis
of unwounded tissue showed that the abundance of each cDNA-
specific transcript changes during fruit ripening and that
each of the transcripts is present in other plant organs as
well. This analysis provides information about the
interactions between developmental and environmental factors
affecting these genes.
215 NAL Call. No.: 442.8 Z8
xpression of mitochondrial genes in fertile and sterile sugar
beet cytop asms with different nuclear fertility restorer
genes!.
udareva, N.A.!; Popovsky, A.V.; Kasjanova, U.V.; Veprev, S.G.;
Mglinets, A.V.; Salganik, R.I.
Berlin, W. Ger. : Springer International; 1991.
heoretical and applied genetics.! v. 83 (2): . 217-224.!
FLD100:English; 1991. Includes references.
Language: nglish!
Descriptors: Beta vulgaris; Mitochondrial genetics;
Cytoplasmic male sterility; Gene expression; Transcription;
Genes; Adenosinetriphosphatase; Cytochrome b; Cytochrome-c
oxidase; Mitochondrial DNA; Molecular mapping; Line
differences; Fertility
Abstract: Variations in mitochondrial genome organization and
in its expression between fertile, sterile sugar beet lines
and fertile nuclear-restored plants were studied. Southern
blot hybridization with COXI, COXII, COB and atpA
mitochondrial genes as probes showed that changes in the
mitochondrial genome organization of sterile lines are
associated with variations in the location of COB, atpA and
COXII, but not COXI. When the COXII and atpA genes were used
as hybridization probes, differences in the primary structure
of mitochondrial DNAs from sterile lines of different origin
were revealed. Differences in the transcriptional patterns of
the three mitochondrial genes (COXI, COXII and atpA) were
observed between fertile and sterile sugar beet lines; COB was
the only mitochondrial gene whose transcription was identical
in both fertile and sterile cytoplasms. The dominant nuclear
fertility restorer genes altered the transcriptional patterns
of the COB and atpA without affecting those of the COXI and
COXII genes; atpA expression was identical in fertile plants
and nuclear-restored plants with sterile cytoplasm.
Author Index
Abu-Abeid, M. 114
Adam, Z. 40
Adamska, I. 30
Aguilar, M. 10
Alefs, S.J.H.M. 108
Amselem, J. 118
An, G. 101, 186
Anderson, E.J. 22
Andrews, T.J. 190
Apel, I.J. 176
Apuya, N.R. 88
Armstrong, G.A. 112
Arnim, A. von 107
Arvidsson, Y.B.C. 190
Atabekov, J.G. 77
Ausubel, F.M. 46
Ayte, J. 27
Bacot, K.O. 196
Baden, C. 65
Baggett, J.R. 100
Balazs, E. 70
Barg, R. 49
Barroso, J. 47
Barry, G.F. 37
Bartley, G.E. 121, 196
Bate, N.J. 69
Batschauer, A. 107
Battraw, M.J. 150, 204
Baumgartner, C. 211
Beachy, R.N. 206
Becker, T.W. 133
Becker-Andre, M. 183
Beer, S.V. 68
Begum, D. 150
Bejarano, E.R. 64
Bell, E. 113
Bennett, A.B. 36, 149
Berlin, J. 58
Bevan, M. 80
Bhairi, S. 26
Bhatt, A.M. 193
Bhattacharyya, M. 25
Bidney, D. 116
Bino, R.J. 103
Bird, A. 33
Bird, C. 33
Bisanz-Seyer, C. 135
Bisseling, A. 143
Bisseling, T. 92
Block, A. 112
Boersig, M. 62
Bogaerts, P. 45
Bogusz, D. 206
Boller, T. 179
Bonas, U. 73, 76, 158, 159
Booij, H. 19
Borkird, C. 180
Botterman, J. 58
Bourguignon, J. 111
Bourque, J.E. 188
Boutry, M. 45
Bouzayen, M. 90
Bowles, D.J. 139
Boyer, C.D. 189
Bozak, K.R. 14
Brady, C.J. 117
Bramley, P. 33
Bransom, K.L. 157
Brasileiro, A.C.M. 8
Braun, C.J. 63
Braun, H.P. 6, 39
Bray, E.A. 132, 134, 136, 212
Brears, T. 155
Brennicke, A. 38
Bressan, R.A. 169
Broglie, K. 163
Broglie, R. 163
Bruneau, J.M. 62
Buck, K.W. 64
Burrell, M. 64
Burrus, M. 116
Bustos, M.M. 150, 204
Butt, A.D. 126
Caboche, M. 108, 133, 197
Camara, B. 89
Campbell, A.D. 1
Carrasco, P. 43
Carrayol, E. 133
Cashmore, A.R. 129
Cass, L.G. 14
Chamovitz, D. 121
Chandler, D. 4
Chen, R.D. 54
Cherel, I. 108
Chern, M.S. 32
Chiang, C.C. 67
Chino, M. 187
Choudhary, A.D. 145
Christoffersen, R.E. 14, 174
Chua, N.H. 48
Citterio, S. 140
Cohen, A. 132, 134, 136
Colombo, B.M. 140
Comai, L. 18, 59
Conrads-Strauch, J. 158, 159
Cornelissen, B.J.C. 97
Coruzzi, G.M. 155
Cosset, A. 95
Costa, M.A. 101, 186
Cuppels, D.A. 23
Da Costa e Silva, O. 112
Dangl, J.L. 53
Daniel-Vedele, F. 197
Darby, R. 213
Dart, P.J. 109
Davidse, L.C. 91
Davis, R.W. 181
Day, A.G. 64
Deforce, L. 93
Delcasso-Tremousaygue, D. 130
DellaPenna, D. 149
Dellapenna, D. 166
Delseny, M. 21, 130
Depigny, D. 21
DeRocher, A.E. 61
Dietrich, A. 95
Dietrich, R.A. 59
Dincher, S. 4
Dixon, R.A. 31, 145
Dolja, V.V. 77
Dong, J.G. 36, 98
Dong, X. 46
Dorbe, M.F. 197
Douce, R. 111
Douglas, C.J. 53
Draper, J. 20, 213
Dreher, T.W. 157
Dron, M. 79
Drory, A. 123
Dry, I. 25
Dudits, D. 70
Dumas, C. 141
Dunn, P. 25
Dunsmuir, P. 65
Dwyer, K.G. 184
Dymock, D. 164
Echeverria, M. 130
Edwards, A. 25
Eimert, K. 199
Ellard, M. 53
Elliott, R.C. 15
Ellis, P.J. 170
Elzen, P.J.M. van den 97, 153
Emmermann, M. 6, 39
Engstrom, P. 180
Falk, A. 86
Farmer, E.E. 165
Farrens, D. 93
Fauquet, C. 206
Fedorkin, O.N. 77
Feher, A. 70
Ferrant, V. 45
Fink, G.R. 46, 208
Fischer, R.L. 10, 149
Folk, W.R. 188
Forster, H.H. 42
Fraley, R.T. 7
Franche, C. 206
Franz, G. 198
Frommer, W.B. 41
Fukui, T. 57, 151
Furuya, M. 93
Gallo-Meagher, M. 15, 142
Galun, E. 195
Gast, R.T. 24
Gatz, C. 106
Gauly, A. 107
Gausman, H.W. 156
Gaynor, J. 163
Gelvin, S.B. 127
Gerrits, W.F.M. 108
Gielen, J.J.L. 51
Gil-Gomez, G. 27
Gilmartin, P.M. 48
Giovannoni, J.J. 149, 166
Glagotskaya, T.Ts 201
Glanz, J. 12
Gleba, Yu.Yu 201
Godoy, J.A. 152
Goldbach, R. 74, 82
Goldbach, R.W. 51
Goldsbrough, P.B. 55
Goldstein, A.H. 147
Gonsalves, D. 66
Goodman, H.M. 148
Gopalraj, M. 24
Goupil, P. 198
Govers, F. 28
Graham, I.A. 99
Granell, A. 129
Gray, J. 119, 127
Grellet, F. 21
Grierson, D. 33, 90, 119
Grinsven, M.Q.J.M. van 51
Grisvard, J. 79
Gruissem, W. 29, 43, 49, 56
Guilluy, C.M. 141
Gurr, S.J. 139
Gutfinger, T. 194
Haan, P. de 51, 82
Haaren, M.J.J. van 182
Habu, Y. 185
Hacker, D.L. 207
Hadwiger, L.A. 67
Hahlbrock, K. 53, 112, 144, 183
Haley, A. 168
Haley, L. 7
Hall, R.B. 200
Hall, T.C. 150, 204
Hamilton, A.J. 90
Hampton, R.O.R 100
Handa, A.K. 11, 124
Hanson, A.D. 177
Harada, H. 105
Harada, J.J. 59
Harada, T. 85
Hardison, R.C. 189
Hareven, D. 115, 194
Harikrishna, K. 213
Harmsen, H. 28
Haro, D. 27
Harriman, R.W. 11, 124
Harrison, M.J. 145
Hart, E.R. 200
Hasegawa, P.M. 169
Hashimoto, T. 125, 202
Hatzopoulos, P. 198
Hauffe, K.D. 53
Hawkins, F.K.L. 171
Hayford, M.B. 37
He, Z. 122
Head, K. 168
Hegardt, F.G. 27
Heidstra, R. 28
Heizmann, P. 141
Helm, K.W. 61
Hemenway, C.L. 63
Hempel, F.D. 198
Hendriks, T. 138
Hennig, N. 194
Hepburn, A.G. 87
Herbers, K. 158, 159
Herminghaus, S. 58
Heupel, R.C. 59
Heyer, A. 106
Higashi, K. 105
Hightower, R. 65
Hinchee, M.A. 7
Hinman, S.B. 189
Hinojos, C.M. 17
Hirai, M. 5
Hirel, B. 133
Hirschberg, J. 121
Hoekema, A. 153
Hoffman, N.E. 40, 110
Hontelez, J. 92
Horicke-Grandpierre, C. 104
Horovitz, D.O 67
Horsch, R.B. 7
Horvath, B. 92
Houck, C.M. 167, 182
Howlett, B. 13
Huang, L. 40
Huang, P.L. 209
Hudson, G.S. 190
Huffman, G. 116
Hugueney, P. 89
Huisman, M.J. 74
Hummel, S. 41
Hungria, M. 9, 50, 172
Hunt, D.F. 122
Huttinga, H. 74
Ichinose, Y. 202
Iida, A. 203
Ireland, R. 34
Ishikawa, H. 131
Ites-Morales, M.E. 53
Ito, N. 93
Izutsu, S. 202
Jacobsen, E. 60
Jenkins, G.I. 81
Johnson, R.R. 165
Johnston, A.W.B. 50, 171
Jones, J.D. 55
Jongedijk, E. 97
Joos, H.J. 144
Joseph, C.M.� 9, 172
Jouanin, L. 8
Judelson, H.S. 191
Kado, C.I. 96
Kalkan, F.A. 150, 204
Kamada, H. 105
Kamdar, H.V. 96
Kammen, A. van 19, 28, 92
Kamoun, S. 96
Kandasamy, M.K. 5, 71
Kaniewski, W. 7
Karasev, A.V. 77
Kasjanova, U.V. 215
Kato, H. 202
Katsube, T. 57
Kaufmann, A. 173
Kaufmann, H. 178
Kawamata, S. 202
Kazuta, Y. 57
Keith, B. 46
Keithly, J.H. 156
Keller, B. 211
Keller, J.A. 1
Kellmann, J.W. 42
Kenigsbuch, D. 49
Kennedy, C. 171
Kernan, A. 200
Kiehne, K. 18
Kim, S. 126
Kim, S.R. 101, 186
Kim, W.T. 36, 98
Kim, Y. 101
Kinoshita, T. 85
Kishore, G.M. 37
Kiyosue, T. 105
Klee, H.J. 37
Klein, B. 104
Klopfenstein, N.B. 200
Kloppstech, K. 30, 192
Knight, M.R. 81
Knighton, M.L. 52
Knoop, V. 73
Knowler, J.T. 193
Ko, K. 110
Komeda, Y. 187, 203
Koning, A.J. 18
Kononowicz, A.K. 169
Kool, A.J. 51
Koornneef, M. 108
Kop, D. van der 108
Kormelink, R. 82
Kossel, H. 107
Kossmann, J. 35
Kozik, A.V. 143
Kretzmer, K.A. 37
Kruft, V. 39
Kull, B. 173
Kuntz, M. 89
Lalonde, B.A. 184
Lamb, C.J. 31, 145
Lancaster, J. 164
Landsmann, J. 58
Lauzon, L.M. 61
Lawson, E.C. 7
Lay-Yee, M. 52
Leaver, C.J. 99
Lee, S.W. 162
Leede-Plegt, L.M. van der 103
Lenman, M. 86
Leple, J.C. 8
Levi, M. 140
Leyva, A. 31
Li, L. 36
Li, N. 3
Liang, X. 31
Lichtenstein, C.P. 64
Lifschitz, E. 114, 115, 194
Lin, X. 32
Lin, X.Y. 41
Link, G. 175
Lippok, B. 38
Liu, D. 3
Liu, X.J. 78
Lloyd, A.M. 181
Loake, G.J. 145
Lou, H. 94
Lukasheva, L.I. 77
Lund, P. 65
Ma, S.W. 23
Mache, R. 135
Macherel, D. 111
Macheroux, P. 72
MacKenzie, D.J. 84, 170
Mahe, A. 79
Makaroff, C.A. 176
Mamiya, G. 137
Manzara, T. 43
Marechal-Drouard, L. 95
Margossian, L. 10
Marrero, P.F. 27
Martich, J. 116
Martin, C. 25
Martineau, B. 167
Massey, V. 72
Masson, J. 95
Matsuda, J. 125
Matsudaira, K.L. 59
Matsui, K. 137
Matsuno, R. 131
Matthews, B.F. 161
Mattoo, A.K. 3, 214
Mattsson, J. 180
Mauch-Mani, B. 4
Maunders, M. 33
Mavandad, M. 145
McBride, K.E. 167
McCarthy, J.E.G. 58
McCue, K.F. 177
McCullough, A.J. 94
McGarvey, D.J. 174
McNabb, H.S. Jr 200
McPherson, J. 84
McPherson, M.J. 139
Mehdy, M.C. 17
Meins, F. Jr 179
Memelink, J. 48
Mglinets, A.V. 215
Michel, H. 122
Michel, M.F. 8
Michelet, B. 45
Michelmore, R.W. 191
Michielsen, P. 28
Mikami, T. 85
Milkowski, D. 110
Mindrinos, M.N. 146
Miranda, J. 128
Miroshnichenko, N.A. 77
Molendijk, L. 153
Montagu, M. van 148
Morell, M.K. 190
Mori, H. 151
Morikawa, H. 203
Morozov, S.Yu 77
Morris, B. 168
Morris, T.J. 207
Morris, V.L. 23
Moses, M.S. 132, 136
Moureau, P. 33
Moyer, M. 4
Muller-Rober, B. 35, 102
Mullet, J.E. 113
Muzzin, J. 8
Nacken, W. 114
Nagano, Y. 131
Nagy, B.P. 1
Naito, S. 187
Nakamaura, K. 120
Nasrallah, J.B. 5, 13, 71, 184
Nasrallah, M.E. 5, 71, 184
Nazar, R.N. 162
Nelson, D.E. 169
Neuburger, M. 111
Neuhaus, J.M. 179
Newell, C.A. 7
Nickelsen, J. 175
Nishio, T. 5, 71
Niyogi, K.K. 208
Nyman, M. 205
Oakes, J.V. 154
Oeller, P.W. 1
Ogren, W.L. 75
Ohad, I. 192
Ohno, T. 185
Ohshima, T. R187
Okabe, S. 125
Oliveira, M.M. 47
Olszewski, N.E. 24
Ooms, G. 164
Ooyen, A.J.J. van 153
Orozco, E.M. Jr 75
Ortiz, R. 16
Otto, B. 192
Ounnoughi, D. 8
Ozeki, Y. 137
Padilla, J.E. 128
Pais, M.S.S. 47
Palmer, J.D. 176
Panopoulos, N.J. 146
Paolillo, D.J. 71
Park, K.Y. 123
Parks, J.E. 209
Parsons, B.L. 3, 214
Paszkowski, U. U53
Pater, S. de 164
Paul, E. 213
Pawlowski, K. 104
Pecker, I. 121
Pelletier, G. 95
Peloquin, S.J. 16
Pen, J. 153
Pena-Cortes, H. 2, 78
Penarrubia, L. 10
Penzes, E. 65
Percival, F.W. 14
Pereto, J.G. 129
Perez, C. 45
Perl-Treves, R. 195
Peter, G.F. 1
Peters, D. 51, 82
Petty, I.T.D. 207
Peyachoknagul, S. 185
Phillips, D.A. 50, 172
Pichersky, E. 42, 110
Picton, S. 119
Piechulla, B. 42
Pieterse, C.M.J. 91
Pintor-Toro, J.A. 31, 152
Plant, A.L. 132, 136
Pnueli, L. 114
Popovsky, A.V. 215
Potter, S. 4
Powell, D.A. 162
Prakash, C.S. 83
Preiszner, J. 70
Pri-Hadash, A. 115
Prins, M. 28
Prufer, D. 173
Quax, W.J. 153
Quemada, H.D. 66
Rahme, L.G. 146
Ramamohan, G. 11
Rask, L. 86
Rawsthorne, S. 34
Ray, J. 33
Raynal, M. 21
Richards, C.M. 189
Richardson, K. 168
Rietveld, K. 153
Risiott, R. 164
Risseeuw, E.P. 91
Robb, J. 162
Roberts, K. 139
Roby, D. 163
Rocha-Sosa, M. 41
Rochon, D.M. 160
Rodrigues-Pousada, R.A. 148
Rohde, W. 173
Romer, S. 89
Ross, G.S. 52
Rost, T. 18
Rothstein, S.J. 69
Rottmann, W.H. 1, 209
Rozman, R. 7
Ryals, J. 4
Ryan, C.A. 165, 210
Sakata, Y. 185
Salganik, R.I. 215
Salm, T.P.M. van der 103
Salts, Y. 49
Samac, D.A. 44
Sanchez, F. 128
Sanchez-Serrano, J.J. 2
Sanders, P. 7
Sasaki, Y. 131
Sato, T. 5, 71
Satoh, S. 105
Scelonge, C. 116
Schantz, R. 89
Scheel, B. 30
Schell, J. 104
Schellekens, G.A. 19
Schena, M. 181
Scheres, V. 143
Schindler, U. 129
Schmid, R. 78
Schmitz, J. 173
Schmitz, U.K. 6, 39
Schoelz, J.E. 22
Schoenmakers, H.C.H. 108
Schopke, C. 206
Schreier, P.H. 58
Schuch, W. 33, 119
Schuler, M.A. 94
Schulte, R. 76
Schulze-Lefert, P. 183
Schuster, G. 29
Schutter, A.A.J.M. de 97
Schwartz, E. 42
Schwarz-Sommer, Z. 114
Scolnik, P.A. 121, 196
Scott, K.F. 109
Scott, R. 20
Sehgal, O.P. 22
Seki, M. 203
Senda, M. 85
Serrano, J.S. 78
Sgorbati, S. 140
Shabbeer, J. 119
Shah, D.M. 44
Shahar, T. 194
Sharma, Y.K. 17
Shen, J.B. 75
Shen, N.F. 1
Shewmaker, C.K. 154
Shi, L. 24
Shi, N.Q. 200
Shinozaki, K. 105
Shiraishi, T. 202
Showalter, A.M. 126
Shul'ga, O.A. 201
Shulga, O.A. 70
Shyr, Y.Y.J. 87
Sidorov, V.A. 201
Siegemund, F. 199
Sijmons, P.C. 153
Silverstone, A. 98
Sims, L. 116
Singh, N.K. 169
Sirevag, R. 174
Skryabin, K.G. 70, 201
Slightom, J.L. 66
Slusarenko, A. 4
Small, I. 95
Smallwood, M.F. 139
Smith, A. 25
Smith, S.M. 99
Sneath, B.J. 68
Solovyev, A.G. 77
Song, P.S. 93
Sonnewald, U. 35, 102
Sowinski, D.A. 15, 142
Spano, A.J. 122
Sparvoli, E. 140
Speirs, J. 117
Sriprasertsak, P. 202
Stalker, D.M. 154
Staples, R.C. 26
Staskawicz, B. 73
Sterk, P. 19
Sticher, L. 179
Stiekema, W.J. 138
Stolte, A. 60
Stolte, T. 97
Straeten, D. van der 148
Suga, T. 137
Sugiura, M. 85
Suire, C. 89
Summerfelt, K. 62
Sung, Z.R. 198
Tabaeizadeh, Z. 54
Tacke, E. 173
Tada, A. 202
Takishima, K. 137
Tanaka, Y. 202
Tanimoto, E.Y. 18
Tanizawa, K. 57, 151
Taylor, L.P. 1
Tepfer, M. 118
Theologis, A. 1, 209
Thiele, D.J. 72
Thompson, G.A. 36
Thompson, J.E. 69
Thompson, W.F. 15, 142
Thornburg, R.W. 200
Thorsness, M.K. 5
Tieman, D.M. 11, 124
Tikhonovich, I.A. 143
Tillson, P. 164
Timko, M.P. 122
Tobias, C.M. 13
Tola, E. 96
Tomizawa, K.I. 93
Topfer, R. 104
Toriyama, K. 71
Torres-Schumann, S. 152
Tremaine, J.H. 84
Trese, A.T. 22
Trick, M. 141
Truesdale, M. 33
Tsuboi, S. 137
Tsukaya, H. 187
Tucker, W.T. 109
Tumer, N.E. 7
Tunen, A.J. van 103
Turano, F.J. 161
Turner, S.R. 34
udareva, N.A.! 215
Uknes, S. 4
Umemoto, K. 185
Upadhyaya, N.M. 109
Varadarajan, U. 83
Ven, B.C.E. van de R103
Veprev, S.G. 215
Vierling, E. 61
Viitanen, P.V. 121, 196
Visser, R.G.F. 35, 60
Voelker, T.A. 62
Volokita, M. 72
Vreugdenhil, D. 138
Vries, S.C. de 19
Wachs, R. 49
Walker, E.L. 155
Wallin, A. 205
Wang, J. 127
Wang, Y. 55
Wanner, L.A. 56
Ward, E. 4
Warner, S.A.J. 20
Watson, J.M. 109
Wei, N. 207
Wei, Z.M. 68
Weil, J.H. 89, 95
Weiland, J.J. 157
Weisshaar, B. 112
Weller, S.C. 55
Widholm, J.M. 87
Wilk, F. van der 74
Williams, S. 4
Willink, D.P.L. 74
Willmitzer, L. 2, 35, 41, 78, 102
Wilson, B.J. 161
Wingate, V.P.M. 210
Wissinger, B. 38
Woodson, W.R. 123
Worrell, A.C. 62
Xue, J. 86
Xuei, X. 26
Yamada, M. 137
Yamada, T. 202
Yamada, Y. 125, 203
Yamaguchi-Shinozaki, K. 105
Yang, S.F. 36, 98
Yang, W.C. 92
Yip, W.K. 36, 98
Yoder, O.C. 26
Yokoyama, H. 156
Yoshida, N. 120
You, R. 198
Zakharyev, V.M. 201
Zakharyev, V.M. 70
Zalenskii, A.O. 143
Zamir, D. 114
Zelenina, D.A. 77
Zhan, X.G. 168
Zimmerman, J.L. 32, 88
Subject Index
(s)-2-hydroxy-acid oxidase 72
Abiotic injuries 2, 3, 20, 52, 53, 113, 123, 126, 129, 167,
186, 195, 208, 213, 214
Abscisic acid 2, 24, 54, 105, 126, 132, 134, 136, 152, 198,
212
Acc 1, 3, 36, 52, 98, 123
Acid anhydride hydrolases 115
Acid phosphatase 147
Actin 79
Actinidia deliciosa 47
Active transport 6
Acyltransferases 62
Adaptation 169
Adenosinetriphosphatase 45, 215
Adp 6
African cassava mosaic geminivirus 168
Agrobacterium 128
Agrobacterium rhizogenes 8, 118
Agrobacterium tumefaciens 7, 8, 41, 58, 59, 60, 70, 71, 84,
94, 116, 127, 164, 169, 180, 186, 199, 200
Agronomic characteristics 11, 97
Air temperature 191, 192
Alcohol oxidoreductases 104
Alleles 16
Alpha-amylase 153
Alternaria solani 44
Amino acid sequences 1, 4, 6, 13, 17, 18, 19, 20, 21, 24, 25,
26, 27, 28, 29, 32, 33, 34, 35, 36, 37, 38, 39, 45, 46, 49,
52, 55, 62, 81, 85, 86, 89, 90, 91, 93, 98, 104, 105, 106,
107, 109, 110, 111, 112, 113, 114, 115, 120, 121, 122, 123,
127, 132, 133, 134, 135, 136, 137, 144, 148, 151, 152, 162,
167, 176, 177, 179, 183, 184, 185, 189, 194, 196, 208, 209
Amino acids 46, 68, 104, 146
Ammonium 68
Amplification 55, 87
Anaerobic conditions 148
Anthers 5, 141
Anthocyanidins 9, 50
Anthocyanins 50
Antigens 140
Antirrhinum 114
Antisense DNA 10, 11, 188
Antisense RNA 12, 102, 119
Apical meristems 18, 19, 115, 116, 194
Apples 36
Arabidopsis 21, 114
Arabidopsis thaliana 4, 13, 27, 44, 46, 86, 148, 181, 184,
187, 203, 206, 208
Asparagus officinalis 20, 213
Aspartate aminotransferase 161
Aspergillus nidulans 79
Atp 6, 75
Autoradiography 47
Auxins 98
Axils 18, 138
Azotobacter vinelandii 171
Bacillus licheniformis 153
Bean leaf roll luteovirus 100
Beta vulgaris 85, 177, 215
Beta-amylase 120
Beta-glucuronidase 5, 8, 41, 44, 53, 60, 99, 103, 116, 150,
164, 168, 169, 180, 182, 198, 203, 205, 206, 211
Betaine 177
Binding proteins 29, 129, 130, 175
Binding site 29, 43, 48, 57, 75, 112, 129, 175, 194
Biochemical pathways 196
Biological development 29
Biosynthesis 1, 23, 46, 58, 89, 90, 93, 171, 190, 196
Biotypes 92
Blight 91
Blood proteins 65
Brassica campestris 71, 96, 207
Brassica campestris var. rapa 22
Brassica juncea 96
Brassica napus 59, 71, 86, 203
Brassica napus var. oleifera 5, 21
Brassica oleracea 5, 71, 96, 141, 184
Brassica oleracea var. botrytis 199
Brassica oleracea var. viridis 5
Bremia lactucae 191
Buds 18, 138, 184
Cadaverine 58
Cajanus cajan 109
Callus 83, 88, 147, 198, 202, 205
Capsicum annuum 73, 76, 89, 158, 159
Capsicum frutescens 96
Carbohydrate metabolism 11, 35, 62, 102
Carbohydrates 145, 154
Carboxy-lyases 34, 58
Carboxypeptidases 167
Carotenoids 121, 196
Catechol oxidase 194
Cauliflower mosaic caulimovirus 22
Cell differentiation 26, 115, 213
Cell division 18, 213
Cell growth 140
Cell lines 55, 147
Cell suspensions 19, 87, 139, 147, 161, 202, 213
Cell ultrastructure 71
Cell wall components 28, 53, 126, 129, 145, 211
Cell walls 11, 149
Characterization 109, 111
Chemical composition 89
Chemical reactions 11
Chemoreceptors 181
Chenopodium amaranticolor 207
Chimeras 5, 22, 41, 44, 60, 70, 83, 102, 103, 145, 149, 200,
211
Chitinase 44, 79, 163, 179
Chloramphenicol acetyltransferase 47, 145, 186, 188, 202
Chlorates 108
Chlorophyll a/b binding protein 30, 40, 42, 107
Chloroplast genetics 29, 69, 131, 148, 175, 189
Chloroplasts 29, 30, 40, 58, 69, 107, 110, 131, 175, 189, 192
Chlorosis 108
Chromosome maps 208
Chromosome number 16
Chymotrypsin inhibitors 185
Cinnamic acid 145
Circadian rhythm 30, 192
Citrates 146
Clones 54, 111, 144, 193, 207
Cloning 17, 21, 27, 29, 32, 34, 35, 36, 37, 52, 57, 58, 74,
89, 94, 110, 120, 121, 123, 124, 125, 131, 137, 148, 151, 160,
167, 177, 183, 209, 214
Coat proteins 7, 66, 70, 74, 84, 97, 168, 170, 201, 207
Coenzyme a 183
Coenzymes 108
Colletotrichum lindemuthianum 17, 79, 145
Comparisons 1, 17, 109
Complementation 108, 197
Controlling elements 15, 31, 48, 112, 129, 182, 186, 198, 211
Copper 194, 195
Corolla 99, 123, 169
Cortex 18
Cotyledons 43, 56, 99, 133, 150, 180, 204
Coumaric acids 183
Crop quality 16
Crop yield 156
Crosses 100
Crown gall 8, 164
Cucumber mosaic cucumovirus 66
Cucumbers 160
Cucumis sativus 99, 118, 179
Cucurbita pepo 209
Cultivars 67, 97, 201
Cuphea 104
Cycloheximide 209
Cytochrome b 215
Cytochrome c 39
Cytochrome-c oxidase 38, 85, 176, 215
Cytology 213
Cytoplasm 161
Cytoplasmic male sterility 85, 176, 215
Dark 106
Datura stramonium 96
Daucus carota 19, 32, 38, 87, 88, 105, 129, 161, 180, 188,
198
Defense mechanisms 53, 79, 96, 162, 179, 208
Degradation 29
Deletions 31, 129, 145, 175, 186, 211
Deoxyuridine 115
Derivatives 4, 165
Detection 79, 92
Developmental stages 25
Dianthus caryophyllus 123
Differentiation 8
Diploidy 16
Direct DNAuptake 47, 199, 203, 206
Disease resistance 66, 67, 70, 84, 158, 159, 162, 170, 179,
191, 201
Disease transmission 74
Disease vectors 66
Diurnal variation 30, 133
Dna 4, 17, 20, 22, 23, 25, 36, 46, 52, 57, 104, 105, 109,
118, 121, 122, 125, 126, 130, 131, 133, 136, 139, 140, 144,
150, 151, 160, 167, 168, 180, 189, 190, 214
Dna amplification 98
Dna binding proteins 43, 48, 112, 129, 198
Dna conformation 38
Dna footprinting 43
Dna replication 168, 213
Dna sequencing 181
Dominance 67
Drought 132, 136, 195
Drought resistance 54
Dry matter accumulation 102
Dwarfing 22
Electroporation 145, 199
Embryogenesis 19, 21, 59, 105, 150, 198
Environmental factors 164, 191
Enzyme activity 1, 3, 11, 13, 58, 60, 62, 75, 79, 89, 90, 98,
101, 102, 103, 104, 108, 115, 117, 124, 130, 149, 153, 161,
169, 175, 179, 187, 188, 195, 197, 202, 205
Enzyme deficiencies 108
Enzyme inhibitors 165, 200, 210
Enzyme polymorphism 149
Enzymes 196
Epidermis 19, 169
Erwinia amylovora 68
Escherichia coli 57, 109, 148, 171, 190
Esterases 124
Ethephon 195
Ethylene 1, 44, 90, 126, 163, 166, 174, 195, 209, 214
Ethylene production 10, 37, 52, 98, 117, 119, 123
Etiolation 15, 43, 56, 106, 122, 142
Evolution 21, 41
Exons 33, 53, 135, 148, 208
Explants 118
Expressivity 16
Extraction 124
Far red light 133, 142
Ferredoxin 15, 142
Fertility 215
Firmness 37
Flavonoids 9, 50, 143, 172
Flavonols 50
Flowering 2, 114, 115, 194
Flowers 1, 2, 19, 28, 104, 115, 184, 194
Food industry 153
Fragaria ananassa 205
Fructose 68, 146
Fruit 43, 89
Fruiting 18, 167, 169, 182
Fruits 1, 3, 10, 11, 14, 16, 18, 33, 36, 37, 49, 52, 56, 117,
119, 124, 148, 149, 166, 167, 174, 182, 189, 210, 214
Fungal diseases 179
Fusarium oxysporum f.sp. pisi 67
Gas chromatography 47
Gene dosage 87
Gene expression 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,
14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,
29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43,
44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58,
59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73,
74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88,
89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102,
103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114,
115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126,
127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138,
139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150,
151, 152, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162,
163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 174,
175, 176, 177, 179, 180, 181, 182, 183, 184, 185, 186, 187,
188, 189, 190, 191, 192, 193, 194, 195, 196, 197, 198, 199,
200, 201, 202, 203, 204, 205, 206, 207, 208, 209, 210, 211,
212, 213, 214, 215
Gene location 110
Gene mapping 85, 110, 121, 130, 155
Gene transfer 8, 14, 37, 47, 51, 66, 70, 83, 84, 95, 103,
170, 187, 190, 199, 203, 204, 205
Genes 6, 17, 19, 22, 26, 27, 29, 31, 32, 35, 38, 39, 48, 49,
51, 52, 53, 54, 55, 58, 60, 62, 65, 66, 67, 68, 69, 71, 73,
74, 76, 79, 80, 84, 92, 95, 96, 97, 99, 105, 106, 109, 110,
113, 115, 118, 119, 122, 123, 127, 128, 131, 134, 135, 143,
146, 149, 152, 154, 162, 164, 166, 167, 170, 171, 173, 175,
182, 191, 194, 195, 197, 198, 200, 207, 211, 215
Genetic analysis 13, 17, 22, 23, 98, 109
Genetic code 13, 24, 25, 36, 46, 59, 70, 89, 98, 124, 136,
173, 209
Genetic engineering 97
Genetic markers 79, 200
Genetic regulation 1, 2, 3, 14, 15, 16, 20, 23, 24, 27, 36,
40, 41, 45, 48, 53, 56, 59, 61, 68, 69, 71, 73, 78, 80, 81,
88, 99, 105, 110, 112, 113, 117, 119, 124, 126, 128, 132, 133,
134, 136, 142, 143, 145, 147, 149, 150, 152, 162, 164, 166,
167, 169, 174, 185, 186, 187, 190, 195, 197, 198, 208, 210,
211, 214
Genetic resistance 7, 51, 63, 64, 67, 74, 84, 97, 170
Genetic transformation 5, 7, 8, 10, 11, 15, 31, 37, 41, 44,
47, 51, 53, 58, 59, 60, 62, 63, 64, 65, 66, 70, 71, 74, 80,
83, 84, 90, 95, 97, 102, 103, 116, 118, 142, 145, 148, 153,
154, 155, 164, 169, 170, 180, 186, 197, 198, 199, 200, 203,
205, 206, 211
Genetic variance 16
Genetic variation 16, 18, 212
Genistein 50
Genome analysis 82
Genomes 144, 173, 189
Genotype environment interaction 16, 191
Genotypes 16, 83, 191, 212
Germination 59
Gibberellic acid 24
Glucocorticoids 181
Glucose 57, 68, 102
Glutamate-ammonia ligase 133, 155
Glycerol 68
Glycine 34, 111, 126
Glycine max 94, 113, 121, 188
Glycine soja 121
Glycogen (starch) synthase 25, 60
Glycoproteins 5, 71, 126, 129, 138, 184
Glycosyltransferases 154
Glyphosate 55, 87
Greening 131, 192
Growth 24, 171
Growth models 14
Growth rate 156
Growth regulators 156
Gynoecium 5, 18, 167, 169
Hafnia alvei 58
Haploids 16
Heat shock 54, 88, 110, 148, 192
Heat shock proteins 32, 61, 88, 212
Heat stress 61, 152
Heat tolerance 212
Helianthus annuus 116
Herbicide resistance 55, 87
Heritability 16
Hexosyltransferases 35, 102
Histochemistry 96
Histoenzymology 5, 41, 44, 60, 169, 182, 203, 211
Histones 18
Hordeum vulgare 139
Host parasite relationships 17, 23, 67, 79, 84
Host specificity 96, 191
Hybrids 8, 16, 187, 200
Hydro-lyases 148
Hydrolases 37
Hydrolysis 153
Hydroxyproline 126
Hyoscyamus niger 125
Hypersensitivity 76
Hyphae 26, 145
Hypocotyls 98, 113, 150, 156, 180
Ice damage 65
Ice nucleation 23
Idaho 100
Immunocytochemistry 71, 140
In vitro 107, 146
In vitro culture 164
In vitro selection 8, 87, 147
Incompatibility 96
Induced mutations 108
Induced resistance 4, 84, 170
Induction 9, 50, 165, 172
Industrial applications 153
Infection 79
Infections 26, 44
Inheritance 11, 100
Inhibition 3, 65
Injuries 46, 144, 193
Insertional mutagenesis 23
Interactions 50
Interspecific hybridization 16
Introns 26, 38, 81, 85, 122, 135, 148
Ipomoea batatas 83, 120
Isoenzymes 25, 75, 147, 149, 151, 161
Isolation 111
Jasmonic acid 113, 165
Juglans nigra 8
Juglans regia 8
Kanamycin 116
Kinases 190
Klebsiella 154
Laboratory equipment 203
Laboratory methods 204
Lactuca sativa 191
Leaves 2, 15, 19, 27, 37, 41, 43, 44, 54, 56, 60, 62, 65, 69,
78, 79, 81, 99, 104, 106, 108, 109, 111, 113, 116, 122, 126,
133, 134, 135, 139, 141, 148, 164, 167, 168, 169, 193, 194,
199, 203, 206
Leucine 95
Ligases 3, 33, 36, 53, 55, 59, 89, 98, 99, 119, 123, 183
Light 15, 27, 43, 48, 56, 81, 106, 110, 112, 122, 192, 195,
197, 214
Light harvesting complexes 69, 107
Lilium longiflorum 103
Line differences 215
Lines 64, 67
Linkage disequilibrium 16
Lipid metabolism 152
Lipids �137
Lipoxygenase 113
Literature reviews 80, 117, 119, 149, 166
Loci 5, 96, 141, 176
Lyases 46, 209
Lycopersicon 54
Lycopersicon esculentum 1, 2, 3, 10, 11, 12, 18, 23, 24, 33,
37, 40, 42, 43, 44, 49, 56, 59, 62, 65, 76, 90, 108, 110, 114,
115, 119, 124, 126, 132, 133, 134, 136, 139, 147, 148, 149,
152, 158, 159, 162, 165, 166, 167, 182, 189, 194, 195, 196,
197, 212, 214
Lycopersicon peruvianum 210
Lysine 57, 75
Maize starch 153
Major genes 100
Malic acid 59
Maltose 68
Malus pumila 52
Malus sylvestris 36, 98
Manihot esculenta 206
Mannitol 68
Marker genes 83
Mass spectrometry 47
Maturation 169
Mechanical damage 20, 116, 213
Mechanical transmission 66
Medicago sativa 145, 155, 165
Meiosis 16
Melanins 171
Membranes 39, 137
Mesophyll 169, 213
Messenger RNA 1, 2, 3, 5, 11, 15, 17, 18, 19, 20, 21, 26,
28, 29, 30, 32, 33, 35, 36, 38, 39, 42, 49, 52, 54, 55, 56,
61, 65, 69, 79, 81, 85, 86, 87, 88, 92, 99, 102, 105, 106,
108, 110, 111, 112, 113, 118, 119, 122, 123, 126, 131, 133,
135, 141, 142, 143, 144, 148, 152, 156, 162, 165, 167, 174,
175, 176, 177, 182, 184, 189, 192, 193, 194, 195, 197, 208,
213, 214
Metabolites 76
Methionine 188
Microbial proteins 46
Micropropagation 8
Mildews 4
Mineral deficiencies 147
Mitochondria 6, 39, 95, 111
Mitochondrial DNA 38, 85, 176, 215
Mitochondrial genetics 85, 95, 176, 215
Molecular biology 17, 22, 50
Molecular conformation 95, 148, 173
Molecular genetics 82, 90
Molecular mapping 31, 118, 175, 186, 215
Molecular weight 61
Morphogenesis 192
Movement 207
Multigene families 1, 2, 4, 21, 28, 34, 41, 42, 43, 45, 56,
81, 86, 88, 91, 104, 107, 126, 138, 147, 148, 176, 184
Multiple genes 18, 85, 104, 133, 177, 208
Mutagenesis 96
Mutants 16, 23, 24, 31, 40, 93, 96, 108, 109, 115, 128, 149,
157, 160, 166, 171, 190, 194, 197, 207
Mutations 46, 95, 127, 171
Myzus persicae 66, 74
Nadph 122
Naringenin-chalcone synthase 112, 145, 187
Necrovirus group 160
Nicotiana 94, 103, 155, 168, 207
Nicotiana plumbaginifolia 45, 99, 197
Nicotiana sylvestris 179
Nicotiana tabacum 15, 31, 51, 53, 55, 58, 63, 64, 65, 66, 76,
101, 116, 133, 142, 150, 153, 165, 169, 170, 179, 186, 211
Nicotinic acid 4, 68
Nitrate 108, 197
Nitrate reductase 108, 197
Nitrates 171
Nitrogen 68
Nitrogen fixation 92, 128, 171
Nitrogenase 92
Nodulation 9, 128, 143, 172
Nodules 171
Nodulins 92, 128, 143
Nuclei 69, 130
Nucleoproteins 30, 131, 140
Nucleotide sequences 1, 4, 6, 13, 17, 18, 19, 20, 21, 24, 26,
27, 28, 29, 32, 33, 34, 36, 37, 38, 39, 41, 42, 43, 45, 46,
49, 52, 55, 59, 62, 81, 85, 86, 89, 90, 91, 95, 98, 104, 105,
106, 107, 109, 110, 111, 112, 113, 114, 115, 120, 121, 122,
123, 124, 125, 127, 129, 130, 131, 132, 133, 134, 135, 136,
137, 144, 148, 150, 151, 152, 155, 160, 162, 167, 175, 176,
177, 181, 183, 184, 185, 186, 187, 189, 194, 196, 202, 207,
208, 209, 210, 214
Nucleotidyltransferases 35, 57, 102
Nutrient sources 171
Nutrient uptake 147
Nutrition physiology 147
Oscillation 30
Osmolarity 146
Osmotic pressure 177
Ova 16
Overdominance 16
Oxidoreductases 10, 52, 90, 111, 119, 122, 177
Oxo-acid-lyases� 208
Oxygenases 125
P-coumaric acid 145
Paraquat 195
Parenchyma 31, 169
Pathogenesis 26, 162
Pathogenesis-related proteins 4, 17, 20, 169
Pathogenicity 23, 76, 96
Pectinesterase 11, 119
Pectins 11, 124
Peptides 46
Pericarp 169
Peronospora parasitica 4
Persea Americana 14, 174
Petroselinum crispum 53, 112
Petunia 187
Ph 68, 146
Phaseolin 150
Phaseolus vulgaris 9, 17, 31, 50, 69, 79, 81, 95, 128, 145,
150, 163, 172, 204, 211
Phenotypes 22, 109, 118
Phenylalanine ammonia-lyase 31, 144, 162, 202
Phloem 31
Phosphates 147
Phosphorylase 151, 193
Phosphotransferases 8, 116, 199
Photoperiod 138
Photoreceptors 142
Photorespiration 111
Photosystem ii 27, 69
Phytochrome 48, 93, 106, 133, 142
Phytophthora infestans 44, 91, 144
Phytophthora megasperma 53
Phytotoxins 23
Pisum 171
Pisum sativum 15, 18, 25, 28, 30, 34, 48, 61, 67, 92, 94,
100, 107, 111, 122, 131, 140, 142, 143, 155, 192, 202
Plant breeding 16, 70
Plant composition 9, 25, 172
Plant development 19, 43, 56, 80, 102, 138, 148, 156
Plant disorders 109
Plant embryos 19, 25, 59, 88, 105, 180, 198
Plant morphology 118
Plant pathogens 163
Plant physiology 117
Plant proteins 6, 10, 19, 21, 27, 28, 30, 41, 49, 69, 78, 91,
102, 105, 110, 111, 126, 134, 139, 152, 192, 211, 213
Plant secretions 179
Plant tissues 116
Plasma membranes 6, 45, 107, 192
Plasmids 66, 72, 73, 118, 170, 171, 190
Plastids 135, 189
Pollen 5, 103, 169
Pollen germination 169
Polyethylene glycol 47
Polygalacturonase 119, 149
Polymerase chain reaction 94, 141, 143
Polypeptides 26, 27, 120, 174, 179
Polyuronides 11
Populus alba 8, 200
Populus grandidentata 200
Populus tremula 8
Position effect 164
Postharvest physiology 36
Potato leaf roll luteovirus 74, 173
Potato m carlavirus 84
Potato s carlavirus 84
Potato starch 153
Potato x potexvirus 7, 63, 70, 77, 84, 97, 201
Potato y potyvirus 7
Precursors 39
Proline 28, 49
Promoters 5, 15, 28, 31, 33, 41, 42, 43, 44, 48, 53, 58, 101,
110, 112, 129, 130, 135, 145, 150, 164, 168, 169, 180, 182,
186, 198, 202, 206, 211
Protein analysis 161, 210
Protein composition 130, 174
Protein content 130
Protein kinase 13
Protein synthesis 14, 54, 61, 69, 71, 78, 165, 212
Protein transport 39, 58, 107
Proteinase inhibitors 2, 78, 101, 138, 167, 186
Proteinases 165, 200, 210
Proteins 135, 137
Proteolysis 157
Protochlorophyllides 122
Protoplasts 14, 47, 129, 145, 168, 198, 199, 202, 204, 205,
207
Prunus avium 8
Pseudogenes 33
Pseudomonas 37
Pseudomonas syringae 46
Pseudomonas syringae pv. maculicola 208
Pseudomonas syringae pv. phaseolicola 146
Pseudomonas syringae pv. tomato 4, 23, 208
Pseudopleuronectes 65
Psophocarpus tetragonolobus 185
Purification 72, 89, 124, 137, 161
Putrescine 3
Pyrophosphates 89
Quantitative techniques 79
Quantitative traits 16
Races 67
Radicles 180
Raphanus sativus 21, 96, 130, 156, 176
Recessive genes 16, 100, 108
Recombinant DNA 180, 188
Recombination 85, 93, 176
Recrystallization 65
Recurrent selection 16
Red light 133, 142
Regeneration 55, 84
Regenerative ability 7, 83, 205
Regulation 9, 163, 165, 167, 188, 212
Repetitive DNA 21, 42, 176
Replication 74, 207
Reporter genes 5, 8, 41, 44, 47, 53, 60, 99, 103, 116, 145,
150, 164, 168, 169, 180, 182, 186, 188, 198, 199, 203, 206,
211
Resistance 108, 147
Respiration 213
Restriction fragment length polymorphism 110, 121
Restriction mapping 1, 21, 27, 36, 38, 85, 114, 118, 123,
167, 176, 184, 189, 194, 208, 210
Rhizobium 9, 109
Rhizobium leguminosarum 28, 50, 92, 128, 143, 171, 172
Rhizobium meliloti 109
Ribonucleases 175
Ribosomal DNA 69, 213
Ribosomal RNA 69, 213
Ribosomes 30, 88, 131, 135, 156, 173
Ribulose 1,5-diphosphate 190
Ribulose-bisphosphate carboxylase 43, 48, 56, 58, 69, 75, 81
Ricinus communis 137
Ripening 1, 10, 11, 14, 33, 36, 37, 52, 89, 117, 119, 124,
148, 149, 166, 174, 189, 196, 214
Ripening stage 37, 189, 214
Rna 22, 24, 77, 98, 130, 139, 157, 160, 173, 188, 189, 207
Rna editing 38
Rna polymerase 63, 130, 173, 188
Root exudates 50, 172
Root hairs 143
Root meristems 18
Root nodules 28, 92, 128, 143
Root tips 18
Roots 15, 44, 83, 104, 106, 118, 125, 133, 135, 139, 141,
148, 156, 164, 169, 180, 193, 203
Saccharomyces cerevisiae 72, 90, 93
Salicylic acid 3, 44, 101
Salinity 152, 169, 177
Salt tolerance 177
Screening 16, 100
Secretion 147
Seed development 134, 150
Seed germination 9, 135, 140, 155
Seed set 16
Seed treatment 156
Seedling growth 156
Seedlings 15, 30, 106, 108, 131, 137, 152
Seeds 19, 50, 104, 135, 153, 198
Segregation 108
Selection 108
Self compatibility 71
Self incompatibility 5, 71, 141, 184
Senescence 1, 69, 99, 123, 169
Serine proteinases 138
Shoot meristems 150
Shoots 8, 18, 19, 98, 164, 180
Sinapis alba 86, 107, 175
Sodium chloride 152, 169
Solanum 16
Solanum chacoense 16
Solanum phureja 2
Solanum tuberosum 2, 6, 7, 16, 25, 35, 39, 41, 57, 60, 70,
74, 78, 80, 84, 91, 95, 97, 102, 106, 138, 139, 144, 151, 154,
164, 183, 186, 193, 201
Somaclonal variation 147
Somatic embryogenesis 19, 88, 105, 180
Spatial distribution 18, 71
Spatial variation 150, 180
Spermidine 3
Spermine 3
Spinacia oleracea 29, 72, 75, 135, 190
Sprouts 106
Stability 22
Starch 35, 62, 102, 153, 193
Starch granules 60
Starch industry 153
Stems 27, 28, 118, 126, 133, 139, 152, 164, 169, 193, 203,
211
Steroids 181
Stigma 141
Stolons 60, 193
Strain differences 22, 66, 96
Strains 22, 50, 66, 92, 96, 109, 128
Stress 152, 177, 195
Stress response 61, 96, 136, 144
Structural genes 4, 10, 11, 15, 20, 33, 34, 63, 87, 102, 107,
133, 142, 144, 153, 185, 196, 208
Structure activity relationships 111
Styles 5
Suberin 162
Suberization 162
Succinic acid 146, 171
Sucrose 60, 62, 68, 101, 102, 146, 186
Sugars 60, 186, 187
Superoxide dismutase 195
Suppression 96
Symbionts 50
Symbiosis 128
Symptoms 22, 64, 160
Synergism 22
Targeted mutagenesis 190
Temperature 68
Temporal variation 150, 180
Terpenoids 89
Thigmotropism 26
Thin layer chromatography 47
Thioglucosidase 86
Thylakoids 40, 107, 192
Tissue culture 87, 118, 138, 147
Tolerance 100
Tomato golden mosaic geminivirus 64
Tomato spotted wilt virus 51, 82, 170
Tomatoes 149
Transcription 1, 9, 24, 28, 30, 33, 38, 39, 42, 43, 48, 50,
56, 65, 68, 89, 98, 99, 107, 126, 129, 130, 133, 138, 141,
143, 145, 149, 160, 172, 175, 176, 188, 195, 197, 198, 201,
209, 213, 215
Transfer 137
Transfer RNA 95, 188
Transferases 87, 164
Transgenics 5, 7, 8, 10, 11, 15, 31, 37, 41, 44, 51, 53, 58,
59, 60, 62, 63, 64, 65, 66, 71, 74, 80, 83, 84, 95, 97, 101,
102, 142, 150, 153, 154, 155, 164, 168, 169, 170, 180, 182,
186, 187, 197, 198, 200, 201, 205, 206, 211
Translation 77, 88, 107, 156, 157, 173, 195
Translocation 40
Tree breeding 8
Triticum aestivum 94
Tropane alkaloids 125
Tuber sprouting 193
Tubers 2, 16, 25, 35, 41, 60, 78, 80, 102, 138, 154, 193
Tumors 8
Turnip crinkle carmovirus 207
Turnip yellow mosaic tymovirus 157
Udp 57
Ultraviolet radiation 53
Uptake 95
Uromyces appendiculatus 26
Usda 12
Vacuoles 179
Varietal susceptibility 67
Vascular system 211
Vectors 7, 57, 75, 103
Verticillium albo-atrum 162
Vigna radiata 98
Viral antigens 22
Viral proteins 51, 157, 173
Virulence 22, 127, 191
Water stress 54, 113, 126, 134, 136
White light 133, 142
Wild plants 16
Wilting 134
Wilts 162
Xanthine dehydrogenase 108
Xanthomonas campestris pv. armoraciae 96
Xanthomonas campestris pv. campestris 96
Xanthomonas campestris pv. vesicatoria 73, 76, 158, 159
Xanthophylls 192
Xylem 31, 162, 169
Yeasts 93
Zea mays 62
Zinc 195