TITLE: Biotechnology: Gene Expression in Cereal Crops, June 1992 - May
1994, QB 94-57
PUBLICATION DATE: May 1994
ENTRY DATE: November, 1994
EXPIRATION DATE: None
UPDATE FREQUENCY: As needed
CONTACT: Biotechnology Information Center(biotech@nalusda.gov)
National Agricultural Library
DOCUMENT TYPE: Text
DOCUMENT SIZE: 460 K
Gene Expression in Cereal Crops
SEARCH STRATEGY
SET ITEMS DESCRIPTION
S1872 (EXPRESS? (3W)(GENE OR GENES))/TI
S2 9327 GENE(W)EXPRESS?/DE
S3 9568 S1 OR S2
S4 113032 BARLEY OR MAIZE OR CORN OR MILLET OR OAT OR RICE
OR RYE OR TRITICALE OR WHEAT OR SORGHUM OR MILO
OR BUCKWHEAT OR ((CEREAL OR GRAIN)()CROP?)
S5 108166 S4/TI,DE
S6 39947 HORDEUM OR ((AVENA OR ORYZA)()SATIVA) OR
SECALE()CEREALE OR ZEA()MAYS OR TRITICUM()AESTIVUM
S7 117412 S5 OR S6
S8 1201 S3 AND S7
S9391 S8 AND PY=1992:1994
1 NAL Call. No.: QK710.P62
A 168 bp derivative of Suppressor-mutator/Enhancer is responsible for the
maize o2-23 mutation.
Language: English
Descriptors: Zea mays; Transposable elements; Loci; Alleles; Opaque-2 maize;
Structural genes; Dna binding proteins; Exons; Mutations; Mutants;
Mutagenesis; Genetic regulation; Gene expression; Messenger RNA
Abstract: From a directed transposon tagging of the maize Opaque-2 gene (O2),
we have isolated a stable mutant o2 allele, o2-23. Cloning and molecular
analysis of the allele revealed a 168 nucleotide insertion in the third exon
of o2. The sequence of this small insertion indicated identity with the 5' and
3' ends of the 8.3 kb Suppressor-mutator/Enhancer (Spm/En) transposable
element. This represents the smallest deletion derivative of Spm (dSpm) thus
far characterized in maize. Genetic crosses of plants homozygous for o2-23
with plants homozygous for both an o2 null allele (o2-R) and an autonomous Spm
produce stable opaque seed having no apparent sectors of vitreous endosperm.
DNA fragments of the size expected if the dSpm were to excise were not
detectable by Southern analysis, suggesting that this element is unable to
transpose. Northern analysis detected an o2-23 mRNA that was much more
abundant in o2-23 seeds lacking Spm than in o2-23 seeds containing Spm,
consistent with the idea that Spm transacting functions can suppress the
accumulation of the o2-23 transcript.
2 NAL Call. No.: QK710.P68
3'-end processing of the maize 27 kDa zein mRNA.
Wu, L.; Ueda, T.; Messing, J.
Language: English
Descriptors: Zea mays; Gene expression; Messenger RNA; Mutagenesis;
Mutations; Nucleotide sequences; Transcription; Zein
3 NAL Call. No.: QK710.P68
5' distal and proximal cis-acting regulator elements are required for
developmental control of a rice seed storage protein glutelin gene.
Zheng, Z.; Kawagoe, Y.; Xiao, S.; Li, Z.; Okita, T.; Hau, T.; Lin, A.; Murai,
N.
Language: English
Descriptors: Oryza sativa; Transgenics; Transcription; Gene expression;
Glutelins; Seeds; Binding site; Endosperm; Mutations; Promoters
4 NAL Call. No.: 450 P693
Aberrations in plastid transcripts and deficiency of plastid DNA in striped
and albino mutants in maize.
Language: English
Descriptors: Zea mays; Mutants; Plastids; Genome analysis; Gene expression;
Transcription; Dna; Quantitative analysis; Albinos; Protein transport; Genetic
regulation
Abstract: To better understand the regulatory roles of nuclear genes in
chloroplast genomic expression during leaf development in maize (Zea mays L.),
we studied a striped mutant, ii1 (iojap 1), two albino mutants, w1 (white 1)
and w2 (white 2), and their double mutants with 1 (luteus). Homozygous ij1
plants as a female parent produce albino seedlings, called maternal
exceptions, among their progeny, even when the nuclear genotype of the male
parent is normal (+/+). In contrast to albinos that are blocked in the
biosynthetic pathway of carotenoids, w1 and w2 seedlings fall to accumulate
chlorophyll and carotenoids up to the normal level even under dim light
conditions. In ij1-affected plastids, the plastid-encoded proteins and
nuclear-encoded proteins that are associated with thylakoid membranes were not
detecable. However, the 33-kDa protein of the oxygen-evolving complex and
ferredoxin: NADP oxidoreductase, which are localized extrinsically, were
accumulated even though the level of the proteins was decreased. Both ij1 and
w1 albino seedlings contain a normal level of plastid DNA. However, both show
similar aberrant patterns among the transcripts of all the plastid genes
examined (psbB, psbH, petB, petD, atpA, psaB, psbA, and rbcL). Not only were
additional transcripts detected but some of the normal transcripts were not
detectable or were barely detectable by Northern hybridization. These facts
indicate that the transcripts of ij1- and w1-affected plastids may have
altered synthesis, processing or stability. Therefore, the block in expression
of the plastid genome by the nuclear mutants ij1 and w1 may be due to
alterations in the transcriptional or post-transcriptional processes. The fact
that ij1 and maternal-exception progeny show almost identical patterns of
transcripts indicates that the effects of ij1 on plastid gene expression
persist in the subsequent generation even after the nuclear gene, lj1,
restores the normal function. In contrast to ij1 and w1, the levels of all
plastid transcripts in w2 seedlings, whether l or +, are uniformly reduced.
Compared to normal sibling seedlings, the patterns of the RNA species are
relatively unaltered. Relative to the level of a nuclear rDNA, the plastid DNA
content of w2 is decreased 20-fold. Therefore, the limited expression of the
w2-affected plastids may be due to failure to maintain the copy number of
plastid genomes. Thus, albinisms of these mutants result from limiting of
expression of plastids due to alteration of transcripts on the one hand, or to
lowered DNA content on the other.
5 NAL Call. No.: QH506.E46
Abscisic acid is involved in the iron-induced synthesis of maize ferritin.
Lobreaux, S.; Hardy, T.; Briat, J.F.
Language: English
Descriptors: Zea mays; Gene expression; Transcription; Structural genes;
Messenger RNA; Ferritin; Genetic regulation; Abscisic acid; Iron; Nutrient
availability; Stress; Roots; Leaves
Abstract: The ubiquitous iron storage protein ferritin has a highly conserved
structure in plants and animals, but a distinct cytological location and a
different level of control in response to iron excess. Plant ferritins are
plastid-localized and transcriptionally regulated in response to iron, while
animal ferritins are found in the cytoplasm and have their expression mainly
controlled at the translational level. In order to understand the basis of
these differences, we developed hydroponic cultures of maize plantlets which
allowed an increase in the intracellular iron concentration, leading to a
transient accumulation of ferritin mRNA and protein (Lobreaux, S., Massenet,
O. and Briat, J.F., 1992, Plant Mol. Biol, 19, 563-575). Here, it is shown
that iron induces ferritin and RAB (Responsive to Abscisic Acid) mRNA
accumulation relatively with abscisic acid (ABA) accumulation. Ferritin mRNA
also accumulates in response to exogenous ABA. Synergistic experiments
demonstrate that the ABA and iron responses are linked, although full
expression of the ferritin genes cannot be entirely explained by an increase
in ABA concentration. Inducibility of ferritin mRNA accumulation by iron is
dramatically decreased in the maize ABA-deficient mutant vp2 and can be
rescued by addition of exogenous ABA, confirming the involvement of ABA in the
iron response in plants. Therefore, it is concluded that a major part of the
iron-induced biosynthesis of ferritin is achieved through a pathway involving
an increase in the level of the plant hormone ABA. The general conclusion of
this work is that the synthesis of the same protein in response to the same
environmental signal can be controlled by separate and distinct mechanisms in
plants and animals.
6 NAL Call. No.: QH506.E46
Abscisic acid is involved in the iron-induced synthesis of maize ferritin.
Lobreaux, S.; Hardy, T.; Briat, J.F.
Language: English
Descriptors: Zea mays; Gene expression; Transcription; Structural genes;
Messenger RNA; Ferritin; Genetic regulation; Abscisic acid; Iron; Nutrient
availability; Stress; Roots; Leaves
Abstract: The ubiquitous iron storage protein ferritin has a highly conserved
structure in plants and animals, but a distinct cytological location and a
different level of control in response to iron excess. Plant ferritins are
plastid-localized and transcriptionally regulated in response to iron, while
animal ferritins are found in the cytoplasm and have their expression mainly
controlled at the translational level. In order to understand the basis of
these differences, we developed hydroponic cultures of maize plantlets which
allowed an increase in the intracellular iron concentration, leading to a
transient accumulation of ferritin mRNA and protein (Lobreaux, S., Massenet,
O. and Briat, J.F., 1992, Plant Mol. Biol, 19, 563-575). Here, it is shown
that iron induces ferritin and RAB (Responsive to Abscisic Acid) mRNA
accumulation relatively with abscisic acid (ABA) accumulation. Ferritin mRNA
also accumulates in response to exogenous ABA. Synergistic experiments
demonstrate that the ABA and iron responses are linked, although full
expression of the ferritin genes cannot be entirely explained by an increase
in ABA concentration. Inducibility of ferritin mRNA accumulation by iron is
dramatically decreased in the maize ABA-deficient mutant vp2 and can be
rescued by addition of exogenous ABA, confirming the involvement of ABA in the
iron response in plants. Therefore, it is concluded that a major part of the
iron-induced biosynthesis of ferritin is achieved through a pathway involving
an increase in the level of the plant hormone ABA. The general conclusion of
this work is that the synthesis of the same protein in response to the same
environmental signal can be controlled by separate and distinct mechanisms in
plants and animals.
7 NAL Call. No.: QK710.P55
An abscisic-acid-responsive, low temperature barley gene has homology with a
maize phospholipid transfer protein.
Language: English
Descriptors: Hordeum vulgare; Structural genes; Binding proteins; Nucleotide
sequences; Amino acid sequences; Gene expression; Genetic regulation;
Messenger RNA; Abscisic acid; Shoot meristems; Cold tolerance;
Acclimatization
8 NAL Call. No.: QK710.P68
The accumulation of zein polypeptides and zein mRNA in cultured endosperms of
maize is modulated by nitrogen supply.
Language: English
Descriptors: Zea mays; Transcription; Gene expression; Messenger RNA; Zein;
Structural genes; Endosperm; Genetic regulation; Nutrient availability;
Nitrogen; Dna binding proteins; Opaque-2 maize; Protein content; Protein
composition
9 NAL Call. No.: QK710.P62
Activity of a maize ubiquitin promoter in transgenic rice.
Cornejo, M.J.; Luth, D.; Blankenship, K.M.; Anderson, O.D.; Blechl, A.E.
Dordrecht : Kluwer Academic Publishers; 1993 Nov.
Plant molecular biology v. 23 (3): p. 567-581; 1993 Nov. Includes references.
Language: English
Descriptors: Zea mays; Oryza sativa; Promoters; Ubiquitin; Exons; Introns;
Recombinant DNA; Reporter genes; Beta-glucuronidase; Luciferase;
Acyltransferases; Genetic transformation; Transgenic plants; Gene expression;
Callus; Protoplasts; Histoenzymology; Cell division; Enzyme activity;
Herbicide resistance; Bilanafos; Heat shock
Abstract: We have used the maize ubiquitin 1 promoter, first exon and first
intron (UBI) for rice (Oryza sativa L. cv. Taipei 309) transformation
experiments and studied its expression in transgenic calli and plants. UBI
directed significantly higher levels of transient gene expression than other
promoter/intron combinations used for rice transformation. We exploited these
high levels of expression to identify stable transformants obtained from
callus-derived protoplastsco-transfected with two chimeric genes. The genes
consisted of UBI fused to the coding regions of the uidA and bar marker genes
(UBI:GUS and UBI:BAR). UBI:GUS expression increased in response to thermal
stress in both transfected protoplasts and transgenic rice calli.
Histochemical localization of GUS activity revealed that UBI was most active
in rapidly dividing cells. This promoter is expressed in many, but not all,
rice tissues and undergoes important changes in activity during the
development of transgenic rice plants.
10 NAL Call. No.: QD341.A2N8
Activity of yeast FLP recombinase in maize and rice protoplasts.
Lyznik, L.A.; Mitchell, J.C.; Hirayama, L.; Hodges, T.K.
Oxford : IRL Press; 1993 Feb25.
Language: English
Descriptors: Saccharomyces cerevisiae; Zea mays; Oryza sativa; Recombination;
Dna binding proteins; Enzymes; Protoplasts; Dna; Genetic transformation; Gene
expression; Reporter genes
Abstract: We have demonstrated that a yeast FLP/FRT site-specific
recombination system functions in maize and rice protoplasts. FLP recombinase
activity was monitored by reactivation of beta-glucuronidase (GUS) expression
from vectors containing the gusA gene inactivated by insertion of two FRTs
(FLP recombination targets) and a 1.31 kb DNA fragment. The stimulation of GUS
activity in protoplasts cotransformed with vectors containing FRT inactivated
gusA gene and a chimeric FLP gene depended on both the expression of the FLP
recombinase and the presence and structure of the FRT sites. The FLP enzyme
could mediate inter- and intramolecular recombination in plant protoplasts.
These results provide evidence that a yeast recombination system can function
efficiently in plant cells, and that its performance can be manipulated by
structural modification of the FRT sites.
11 NAL Call. No.: QK710.P62
Agrobacterium-mediated production of transgenic rice plants expressing a
chimeric alpha-amylase promoter/beta-glucuronidase gene.
Chan, M.T.; Chang, H.H.; Ho, S.L.; Tong, W.F.; Yu, S.M.
Dordrecht : Kluwer Academic Publishers; 1993 Jun.
Plant molecular biology v. 22 (3): p. 491-506; 1993 Jun. Includes references.
Language: English
Descriptors: Oryza sativa; Agrobacterium tumefaciens; Genetic transformation;
Transgenic plants; Alpha-amylase; Promoters; Recombinant DNA;
Beta-glucuronidase; Phosphotransferases; Reporter genes; Solanum tuberosum;
Cell suspensions; Gene expression; Histoenzymology; Enzyme activity;
Inheritance; Structural genes
Abstract: We have successfully transferred and expressed a reporter gene
driven by an alpha-amylase promoter in a japonica type of rice (Oryza sativa
L. cv. Tainung 62) using the Agrobacterium-mediated gene transfer system.
Immature rice embryos (10-12 days after anthesis) were infected with an
Agrobacterium strain carrying a plasmid containing chimeric genes of
beta-glucuronidase (uidA) and neomycin phosphotransferase (nptII).
Co-incubation of potato suspension culture (PSC) with the Agrobacterium
inoculum significantly improved the transformation efficiency of rice. The
uidA and nptII genes, which are under the control of promoters of a rice
alpha-amylase gene (alpha Amy8) and Agrobacterium nopaline synthase gene
(nos), respectively, were both expressed in G418-resistant calli and
transgenic plants. Integration of foreign genes into the genomes of transgenic
plants was confirmed by Southern blot analysis. Histochemical localization of
GUS activity in one transgenic plant (R0) revealed that the rice alpha-amylase
promoter functions in all cell types of the mature leaves, stems, sheaths and
roots, but not in the very young leaves. This transgenic plant grew more
slowly and produced less seeds than the wild-type plant, but its R1 and R2
progenies grew normally and produced as much seeds as the wild-type plant.
Inheritance of foreign genes to the progenies was also confirmed by Southern
blot analysis. These data demonstrate successful gene transfer and sexual
inheritance of the chimeric genes.
12 NAL Call. No.: QK710.P62
Aleurone nuclear proteins bind to similar elements in the promoter regions of
two gibberellin-regulated alpha-amylase genes.
Rushton, P.J.; Hooley, R.; Lazarus, C.M.
Dordrecht : Kluwer Academic Publishers; 1992 Sep.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 19 (6): p. 891-901; 1992 Sep.
Includes references.
Language: English
Descriptors: Triticum aestivum; Avena fatua; Promoters; Structural genes;
Alpha-amylase; Binding site; Dna binding proteins; Nucleoproteins; Aleurone
cells; Protoplasts; Gene expression; Nucleotide sequences; Controlling
elements; Transcription
Abstract: Binding of nuclear proteins from wild oat aleurone protoplasts to
the promoter regions of two gibberellin-regulated wheat alpha-amylase genes
(alpha-Amy1/18 and alpha-Amy2/54) has been studied by gel retardation and
DNase 1 footprinting. Gel retardation studies using 300-430 bp fragments of
the promoters showed similar binding characteristics with nuclear extracts
from both gibberellin A1-treated and untreated protoplasts. DNase 1 footprints
localised binding of nuclear proteins from gibberellin A1-treated aleurone
protoplasts to regions in both promoters. Similar sequence elements in the
promoter regions of both genes were protected from digestion although the
location and number of footprints in each promoter region were different. Each
footprint contained either a sequence similar to the cAMP and/or phorbol ester
response elements, or a hyphenated palindrome sequence. The presence of cAMP
and/or phorbol ester response element-like sequences in the footprints
suggests that transcription factors of the bZIP type may be involved in the
expression of alpha-amylase genes in aleurone cells. Footprints containing
hyphenated palindrome sequences, found in the promoter regions of both genes,
suggest the possible involvement of other classes of transcription factor. The
conserved alpha-amylase promoter sequence TAACAGA was also shown to bind
nuclear protein in the alpha-Amy2/54 promoter. These observations are
discussed in relation to alpha-amylase gene expression in aleurone and to
functional data concerning these genes.
13 NAL Call. No.: 450 P692
Alteration of gene expression associated with abscisic acid-induced chilling
tolerance in maize suspension-cultured cells.
Xin, Z.; Li, P.H.
Language: English
Descriptors: Zea mays; Cell suspensions; Rna; Protein synthesis; Regulation;
Abscisic acid; Induction; Chilling; Cold tolerance; Gene expression;
Temperature
Abstract: ABA induces chilling tolerance in maize (Zea mays L., cv Black
Mexican Sweet) suspension-cultured cells at 28 degrees C when ABA was added to
the culture medium at least 6 h prior to chilling (4 degrees C), and this
induction can be inhibited by blocking protein synthesis with cycloheximide
treatment (Z. Xin, P.H. Li [1992] Plant Physiol 99: 707-711). De novo
synthesis of proteins and changes in poly(A+) RNAs were investigated during
the ABA induction of chilling tolerance at 28 degrees C as well as during
chilling exposure. At 28 degrees C, ABA increased the net synthesis of 11
proteins. Five of these proteins, whose net synthesis was also increased by
chilling (4 degrees C), were called group I ABA-induced proteins; the
remaining six proteins, whose net synthesis was not altered by chilling, were
called group II ABA-induced proteins. Chilling suppressed the net synthesis of
three proteins. ABA treatment prior to chilling did not alleviate this
suppression. ABA applied at the inception of chilling induced neither chilling
tolerance nor accumulation of any of the group II proteins; however, once the
group II proteins appeared, they were continually synthesized even in a
chilling regimen. ABA induced seven in vitro translation products at 28
degrees C. Three of these products could also be induced by chilling; the
remaining four were induced by ABA only at 28 degrees C. These results suggest
that ABA-induced alteration of protein synthesis at 28 degrees C is associated
with an increased chilling tolerance in maize suspension-cultured cells.
14 NAL Call. No.: QK725.P56 1993
Altered nuclear, mitochondrial and plastid gene expression in white barley
cells containing ribosome-deficient plastids.
Borner, T.; Hess, W.R.
Language: English
Descriptors: Hordeum vulgare; Gene expression; Transcription; Structural
genes; Genomes; Chloroplasts; Mitochondria; Nuclei; Mitochondrial genetics;
Chloroplast genetics; Nucleocytoplasmic interaction; Ribosomes; Deficiency;
Mutants; Messenger RNA
Abstract: The progeny of the barley mutant line albostrians consists of
green, white and green-white striped seedlings. Cells from white tissue
contain plastids which lack ribosomes and, consequently, all proteins encoded
in plastid DNA. In spite of this drastic defect, cells of white leaves have
plastids and plastid DNA in quantities comparable to green leaves. Plastid
genes for ribosomal proteins (rps2, rps15) and subunits of a putative RNA
polymerase (rpoA, rpoB, rpoC1) are transcribed and the mRNAs accumulate to a
distinctly higher level (rps15, rpoB/C1) in white compared to green leaves.
Genes encoding chloroplast proteins involved in bioenergetic functions (psbA,
rbcL, atpI-H), and also tRNA(Glu) and plastid rRNAs, showed little or no
accumulation of their transcripts. The data provide strong evidence for a
plastid RNA polymerase originating entirely from the nucleo-cytoplasmic
compartment. Messengers of mitochondrial genes encoding proteins involved in
respiration (coxII, coxIII, atpA, atp6, cob) were found to accumulate to a
higher level in white vs. green leaves, whereas mitochondrial 18S and 26S
rRNAs were distinctly less affected by the presence of mutant,
undifferentiated plastids. Nuclear genes which are light-induced and normally
specifically expressed in green tissue (rbcS, cab, genes encoding Calvin cycle
enzymes) showed an extremely low accumulation of their mRNAs in white leaves
due to a reduced rate of transcription. Although at a very low level, the
transcription of these genes was still light-inducible, and a circadian rhythm
of cab-mRNA accumulation could be observed. The data are discussed in relation
to regulatory interactions between the genomes of plant cells.
15 NAL Call. No.: QK725.P532
Alternative splicing induced by insertion of retrotransposons into the maize
waxy gene.
Language: English
Descriptors: Zea mays; Transposable elements; Insertional mutagenesis;
Alternative splicing; Structural genes; Nucleotidyltransferases; Alleles; Gene
expression; Introns; Exons; Induced mutations; Messenger RNA; Nucleotide
sequences; Enzyme activity; Endosperm
Abstract: The molecular basis for the low level expression of three alleles
of the maize waxy (Wx) gene has been described. Each allele contains a
retrotransposon in intron sequences. These insertions represent previously
undescribed elements, and their association with three wx alleles indicates
that retrotransposon elements are important agents of spontaneous mutation in
maize. For each allele, element sequences are spliced from pre-mRNA with the
surrounding intron even though the insertions increase intron length by
approximately 40- to 60-fold. In addition, despite differences in element
sequences, insertion sites, and relative orientations, each element disrupts
long-range splice site recognition leading to novel Wx transcripts where exons
both upstream and downstream of the insertion site are skipped. The expression
of wx alleles with large insertions in introns provides support for studies
that indicate that the primary cis requirement for maize introns is the splice
donor and acceptor sites.
16 NAL Call. No.: QK710.P68
Analysis of maize alpha-tubulin gene promoter by transient expression and in
transgenic tobacco plants.
Language: English
Descriptors: Zea mays; Nicotiana tabacum; Transgenics; Beta-glucuronidase;
Gene expression; Genetic analysis; Genetic transformation; Histochemistry;
Promoters; Protoplasts; Tubulin
17 NAL Call. No.: QK710.P62
Analysis of nuclear proteins interacting with a wheat alpha/beta-gliadin and
storage protein gene.
Language: English
Descriptors: Triticum aestivum; Promoters; Structural genes; Gliadin; Binding
site; Dna binding proteins; Nucleotide sequences; Seeds; Seed development;
Gene expression; Genetic regulation
Abstract: The promoter region (-524 to -46) of the wheat alpha/beta-gliadin
seed storage protein gene was analyzed for interactions with nuclear proteins
from developing wheat seeds. Six complexes were detected within the first 165
bp upstream of the transcriptional start site. One of the proteins was a
non-sequence specific AT-binding protein. The remaining five proteins bound in
a sequence specific manner. One (CABP) mapped to a conserved CA-rich element
at -134 to -112 while another (PalBP) mapped to an adjacent, palindromic
sequence at -112 to -106. Three proteins (CTBPs 1-3) formed complexes at two,
independent homologous sites. The activities of four of the binding proteins,
CTBPs 1-3 and CABP, exhibited similar patterns of expression during seed
development: they first appeared at early to mid stages, reached a maximum at
mid stage and subsequently decreased, paralleling the pattern of gliadin mRNA
accumulation. The non-specific AT-binding protein was detected at relatively
high levels only at mid development. PAlBP activity, on the other hand, first
appeared at mid stage and was present at a constant level throughout later
stages of development. The results suggest that the binding proteins may
regulate gliadin expression in an antagonistic manner.
18 NAL Call. No.: QK710.P62
Analysis of the gibberellin-responsive promoter of a cathepsin B-like gene
from wheat.
Language: English
Descriptors: Triticum aestivum; Promoters; Structural genes; Plant proteins;
Cathepsins; Recombinant DNA; Beta-glucuronidase; Reporter genes; Gene
expression; Genetic regulation; Gibberellic acid; Aleurone layer; Nucleotide
sequences; Controlling elements
Abstract: A wheat gene (A121) encoding a protein with sequence similarity to
mammalian cathepsin B is regulated by gibberellic acid (GA) in aleurone layers
of germinating grains. To analyse the mechanism of A121 regulation, its
promoter was fused to the beta-glucuronidase reporter gene (GUS) and
introduced by micro-projectile bombardment into aleurone layers of oat. With
2.3 kb of promoter sequence, the GUS expression was enhanced by GA treatment.
This effect was reversed by abscisic acid (ABA). This result showed for A121,
like the alpha-amylase genes, that the regulation by GA and ABA was at the
level of transcription. The GA responsiveness of the promoter was retained
with as little as 276 bp of promoter sequence. Sequence comparison with a GA
responsive promoter of an alpha-amylase gene identified the conserved element
GCAACGGCAACGATGG which is required intact for full expression of both
promoters. However, there was no identifiable similarity in the cathepsin-like
promoter with the GA-responsive element of alpha-amylase promoters with the
consensus sequence TAACAAA, suggesting that GA affects more than one mechanism
of transcriptional control.
19 NAL Call. No.: QK710.P68
Analysis of three tissue-specific elements from the wheat Cab-1 enhancer.
Gotor, C.; Romero, L.C.; Inouye, K.; Lam, E.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993
Apr.
Language: English
Descriptors: Triticum aestivum; Nicotiana tabacum; Genetic code; Light
harvesting complexes; Chlorophyll a/b binding protein; Gene expression;
Regulation; Light; Transcription; Enhancers; Transgenic plants; Gene mapping;
Nucleotide sequences; Dna footprinting
20 NAL Call. No.: 442.8 Z8
Antisense regulation of the rice waxy gene expression using a PCR-amplified
fragment of the rice genome reduces the amylose content in grain starch.
Shimada, H.; Tada, Y.; Kawasaki, T.; Fujimura, T.
Berlin, W. Ger. : Springer International; 1993 Jul.
Theoretical and applied genetics v. 86 (6): p. 665-672; 1993 Jul. Includes
references.
Language: English
Descriptors: Oryza sativa; Structural genes; Hexosyltransferases; Gene
expression; Genetic regulation; Antisense DNA; Gene transfer; Genetic
transformation; Transgenic plants; Recombinant DNA; Reporter genes;
Beta-glucuronidase; Enzyme activity; Histoenzymology; Amylose; Starch;
Carbohydrate metabolism; Seeds; Callus
Abstract: The waxy gene encodes a granule-bound starch synthase. A 1.0-kb
portion of the sequence of the rice waxy gene, which includes the region
between exon 4 and exon 9, was inserted in an antisense orientation between
the 35 S promoter and the GUS gene of pBI221. The resultant plasmid, pWXA23,
was introduced into rice protoplasts by electroporation. GUS activity was
clearly detected in derived callus lines, suggesting that the antisense
component of the fusion gene was also expressed. Transgenic rice plants were
regenerated from these callus lines and their GUS activity was confirmed. Some
of the rice seeds from these transformants showed a significant reduction in
the amylose content of grain starch, even though they had become polyploid.
These results suggest that even when intron sequences are included, antisense
constructs can bring about a reduced level of expression of a target gene. The
utility of GUS, included as a reporter gene, for the simple detection of
expression of an antisense gene, was apparent from these results.
21 NAL Call. No.: QK710.P62
AT-rich promoter elements of soybean heat shock gene Gmhsp17.5E bind two
distinct sets of nuclear proteins in vitro.
Czarnecka, E.; Ingersoll, J.C.; Gurley, W.B.
Dordrecht : Kluwer Academic Publishers; 1992 Sep.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 19 (6): p. 985-1000; 1992 Sep.
Includes references.
Language: English
Descriptors: Glycine max; Agrobacterium tumefaciens; Helianthus annuus;
Structural genes; Multigene families; Heat shock proteins; Promoters; Binding
site; Dna binding proteins; Nucleotide sequences; Genetic regulation; Gene
expression; Transcription; Alcohol dehydrogenase; Zea mays; Genetic
transformation; Ultraviolet radiation; Chemical reactions
Abstract: A 33 bp double-stranded oligonucleotide homologous to two AT-rich
sequences located upstream (-907 to -889 and -843 to -826) to the start of
transcription of heat shock gene Gmhsp7.5E of soybean stimulated transcription
when placed 5' to a truncated (-140) maize Adh1 promoter. The chimeric
promoter was assayed in vivo utilizing anaerobically stressed sunflower tumors
transformed by a pTi-based vector of Agrobacterium tumefaciens. Nuclear
proteins extracted from soybean plumules were shown to bind double-stranded
oligonucleotides homologous to AT-rich sequences in the 5' flanking regions of
soybean beta-conglycinin, lectin, leghemoglobin and heat shock genes. These
proteins were also shown to bind AT-rich probes homologous to homeobox protein
binding sites from the Antennapedia and engrailed/fushi tarazu genes of
Drosophila. Binding activity specific for AT-rich sequences showed a wide
distribution among various plant organs and species. Preliminary
characterization indicated that two sets of nuclear proteins from soybean bind
AT-rich DNA sequences: a diverse high-molecular-weight (ca. 46-69 kDa) group,
and a low-molecular-weight (23 and 32 kDa) group of proteins. The latter meets
the operational criteria for high-mobility group proteins (HMGs).
22 NAL Call. No.: QK710.P62
Bare-1, a copia-like retroelement in barley (Hordeum vulgare L.).
Manninen, I.; Schulman, A.H.
Language: English
Descriptors: Hordeum vulgare; Retrotransposons; Repetitive DNA; Nucleotide
sequences; Southern blotting; Gene expression; Messenger RNA; Restriction
mapping; Molecular mapping; Amino acid sequences; Plant proteins; Proteinases;
Nucleases; Reverse transcriptase
Abstract: Retroviruses and retrotransposons make up the broad class of
retroelements replicating and transposing via reverse transcriptase.
Retroelements have recently been found to be ubiquitous in the plants. We
report here the isolation, sequence and analysis of a retroelement from barley
(Hordeum vulgare L.) with all the features of a copia-like retrotransposon.
This is named BARE-1 (for Barley Retroelement 1), the first such element
described for barley. BARE-1 is 12 088 bp, with long terminal repeats (LTRs)
of 1829 bp containing perfect 6 bp inverted repeats at their ends and flanked
by 4 bp direct repeats in the host DNA. Between the long terminal repeats is
an internal domain with a derived amino acid sequence of 1285 residues,
bearing homology to the gag, pro, int and rt domains of retroviruses and both
plant and non-plant copia-like retrotransposons. Cultivated barley contains
about 5000 elements in the genome similar to the BARE-1 putative gag domain,
but ten-fold more hybridizing to rt or LTR probes. The particular BARE-1
element reported here appears to be inactive, as the putative protein-coding
domain is interrupted by four stop codons and a frameshift. In addition, the
3' LTR is 4% divergent from the 5' LTR and contains a 3135 bp insertion.
Nevertheless, we have recently detected transcripts hybridizing to BARE-1 on
northern blots, presumably from active copies. Analysis of BARE-1 expression
and function in barley is currently underway.
23 NAL Call. No.: QK710.P62
A barley cDNA clone encoding a type III chlorophyll a/b binding polypeptide of
the light-harvesting complex II.
Language: English
Descriptors: Hordeum vulgare; Multigene families; Structural genes;
Chlorophyll a/b binding protein; Dna; Nucleotide sequences; Amino acid
sequences; Thylakoids; Gene expression; Messenger RNA; Genetic regulation;
Light; Light harvesting complexes
Abstract: The nucleotide sequence of a leaf cDNA clone encoding a Type III
chlorophyll a/b-binding (CAB) protein of light-harvesting complex II (LHCII)
in barley is reported. Sequence comparisons and results from in vitro import
into chloroplasts demonstrate that the cDNA clone encodes a functional transit
peptide of 45 amino acid residues and a mature polypeptide of 223 residues
with a predicted molecular mass of 24.3 kDa. After insertion into thylakoids,
the mature protein is resistant to protease attack. Hybridization analysis
using a gene-specific probe shows that the gene is expressed in dark-grown
seedlings and that the amount of mRNA increases during illumination.
24 NAL Call. No.: 442.8 Z34
Barley embryo globulin 1 gene, Beg1: characterization of cDNA, chromosome
mapping and regulation of expression.
Language: English
Descriptors: Hordeum vulgare; Structural genes; Globulins; Plant embryos;
Complementary DNA; Nucleotide sequences; Amino acid sequences; Gene location;
Chromosomes; Chromosome maps; Gene expression; Messenger RNA; Seed
development; Aleurone layer
Abstract: We report identification of a 2189 bp cDNA clone from barley
corresponding to a single-copy gene, Beg] (Barley embryo globulin), on
chromosome 4, which encodes a storage globulin. In barley, the major protein
reserve in the aleurone layer belongs to the 7S globulin class of proteins
found in many seeds. Electrophoretically and antigenically similar proteins
are present in the barley embryo. Accumulation of Beg1 mRNA was noted
beginning 15-20 days post-anthesis in both the aleurone layer and embryo of
the developing barley grain but not in the starchy endosperm. A high level of
Beg1 mRNA is also present in the mature imbibed aleurones, which can be
repressed by treatment with gibberellic acid. This repressive effect of
gibberellin on the levels of Beg1 mRNA is confirmed in the gibberellin
response-constitutive mutant, slender, whose aleurone layers do not accumulate
Beg1 mRNA even in the absence of applied gibberellic acid. The deduced primary
translation product of the Beg1 mRNA is a 637 amino acid (72 kDa) protein with
homology to maize embryo globulin 1 (GLB1) and a partial sequence of a wheat
7S globulin. The internal amino acid sequence of BEG1 closely matches the
N-terminal sequence of isolated barley aleurone globulin. Seven imperfect
tandem repeats of 16 amino acids each are present near the N-terminus of BEG1,
which conform to the consensus HGEGEREEEXGRGRGR, and contribute to the
observed unusual amino acid composition of this protein. A second, distinct
barley globulin gene, Beg2, which is homologous to maize Glb2, was detected by
Northern and Southern analysis. Beg2 and Beg1 are regulated differently which
may indicate variation in storage or utilization properties among the barley
globulins.
25 NAL Call. No.: QK725.P54
beta-Glucuronidase gene expression and mRNA stability in oat protoplasts.
Higgs, D.C.; Colbert, J.T.
Language: English
Descriptors: Avena sativa; Cell suspensions; Protoplasts; Gene expression;
Messenger RNA; Dna; Electroporation; Plasmids; Gene transfer; Genetic code;
Beta-glucuronidase; Reporter genes; Enzyme activity; Radioactive tracers; Half
life; Transcription; Regulation
Abstract: Protoplasts derived from oat (Avena sativa L.) suspension culture
cells (7 days after subculturing) were electroporated with plasmid DNA
containing the Escherichia coli uidA gene encoding the beta-glucuronidase
reporter enzyme. Consistently high enzyme activity was observed with
electroporation conditions of 500 micro F and 1125 volts/cm. Enzyme activity
and mRNA accumulation time courses were determined. The maximum enzyme
activity was detected at 24 hours after electroporation, while the maximum
mRNA level was detected at 12 hours after electroporation. beta-glucuronidase
mRNA was in vitro synthesized with and without a 5' methylated cap and then
electroporated into protoplasts. Only capped mRNA produced significant enzyme
activity. By electroporating radiolabeled, in vitro synthesized mRNA, the
beta-glucuronidase mRNA half-life was estimated to be approximately 35 minutes
in oat protoplasts.
26 NAL Call. No.: QH442.B5
Bialaphos treatment of transgenic rice plants expressing a bar gene prevents
infection by the sheath blight pathogen (Rhizoctonia solani).
Uchimiya, H.; Iwata, M.; Nojirl, C.; Samarajeewa, P.K.; Takamatsu, S.; Ooba,
S.; Anzai, H.; Christensen, A.H.; Quail, P.H.; Toki, S.
New York, N.Y. : Nature Publishing,; 1993 Jul.
Bio/technology v. 11 (7): p. 835-836; 1993 Jul. Includes references.
Language: English
Descriptors: Oryza sativa; Rhizoctonia solani; Transgenic plants; Genetic
transformation; Disease resistance; Glyphosate; Herbicide resistance; Blight;
Structural genes; Acyltransferases
27 NAL Call. No.: S494.5.B563B554
Biochemical and molecular studies of stress tolerance in barley.
Stanca, A.M.; Terzi, V.; Cattivelli, L.
Wallingford, Oxford, UK : CAB International; 1992.
Biotechnology in agriculture (5): p. 277-288; 1992. In the series analytic:
Barley : genetics, biochemistry, molecular biology and biotechnology / edited
by P.R. Shewry. Includes references.
Language: English
Descriptors: Hordeum; Environmental factors; Stress factors; Stress response;
Genetic regulation; Gene expression; Molecular genetics; Biochemical pathways;
Heat shock; Cold hardening; Drought; Salinity; Heavy metals; Oxygen
28 NAL Call. No.: 450 P692
Bronze-2 gene expression and intron splicing patterns in cells and tissues of
Zea mays L.
Language: English
Descriptors: Zea mays; Genes; Gene expression; Messenger RNA; Introns;
Alternative splicing; Cell culture; Protoplasts
Abstract: A large fraction of the transcripts of the Bronze-2 (Bz2) gene of
maize (Zea mays L.) are unspliced in purple husk tissues. The accumulation of
unspliced messages could have destructive potential if the intron-bearing
mRNAs are translated into aberrant proteins. Our initial studies suggested
that both genetic and physiological factors may influence the degree of
splicing failure. Nuclear background rather than cis-sequence effects is shown
to contribute to the genetic component. The accumulation of unspliced message
does not appear to be directly influenced by diurnal effects on transcript
abundance, by the expression level of the Bz2 gene, or by thermal stress. We
also show that maize cell cultures (Black Mexican Sweet, BMS) can be used to
examine the molecular details involved in splicing failure. Much like whole
maize plants, the BMS cells excise the Bz2 intron with varying degrees of
efficiency. In contrast with heterologous constructs containing plant introns,
splicing of the native Bz2 intron can appproach 100% in BMS cells. Splicing of
transcripts from a marked, introduced gene can be compared to the endogeneous
Bz2 gene facilitating analysis of the impact of sequence changes.
29 NAL Call. No.: QK710.P62
The cab-m7 gene: a light-inducible, mesophyll-specific gene of maize.
Becker, T.W.; Templeman, T.S.; Viret, J.F.; Bogorad, L.
Dordrecht : Kluwer Academic Publishers; 1992 Oct.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 20 (1): p. 49-60; 1992 Oct. Includes
references.
Language: English
Descriptors: Zea mays; Multigene families; Multiple genes; Chlorophyll a/b
binding protein; Gene expression; Messenger RNA; Genetic regulation; Light;
Mesophyll; Etiolation; Nucleotide sequences; Amino acid sequences
Abstract: Southern blot analysis has revealed the existence in maize of
perhaps 12 members of the nuclear cab multigene family encoding the
chlorophyll a- and b-binding proteins of the photosystem II light-harvesting
complex. Hybridization with 3' probes derived from unsequenced cDNA clones
showed that six members of this family differ from one another with respect to
expression in mesophyll and/or bundle sheath cells and regulation by light. An
additional member of this family, designated cab-m7, that encodes a 28 kDa
primary translation product has now been identified. It has been cloned from a
maize genomic library and sequenced to begin to define the bases for
differences in the expression of these genes. This cab gene is shown to be
strongly preferentially expressed in the mesophyll (vs. bundle sheath) cells
of maize. Furthermore, the gene is photo-responsive; although small amounts of
cab-m7 mRNA are present in etiolated leaves, the mRNA pool is 8-fold larger
after six hours of illumination. DNA sequences upstream of the cab-m7 gene
resemble those found in the 5'-flanking regions of some other plant genes.
30 NAL Call. No.: QK710.P62
A cDNA clone for a pathogenesis-related protein 1 from barley.
Muradov, A.; Petrasovits, L.; Davidson, A.; Scott, K.J.
Dordrecht : Kluwer Academic Publishers; 1993 Oct.
Plant molecular biology v. 23 (2): p. 439-442; 1993 Oct. Includes references.
Language: English
Descriptors: Hordeum vulgare; Complementary DNA; Pathogenesis-related
proteins; Nucleotide sequences; Amino acid sequences; Gene expression;
Messenger RNA; Genetic regulation; Fungal diseases; Erysiphe graminis f.sp.
hordei; Ethylene; Salicylic acid; Jasmonic acid; Nicotinic acid; Derivatives
Abstract: A barley cDNA clone (PRb-1) corresponding to an mRNA differentially
induced in resistant compared to susceptible barley cultivars by powdery
mildew infection was isolated and characterised. The deduced amino acid
sequence revealed 24 amino acids comprising the signal peptide and 140 amino
acids of the mature peptide (15 kDa). This showed close homology to PR-1-like
proteins, which have been isolated from maize, tobacco, tomato and Arabidopsis
thaliana. Northern blot analysis showed accumulation of the corresponding mRNA
12 h after inoculation of resistant barley cultivars with Erysiphe graminis.
Increased expression of the PRb-1 gene was also observed in resistant compared
with near-isogenic susceptible barley plants following treatment with
ethylene, salicylic acid, methyl jasmonate and 2,6-dichloro-isonicotinic acid.
31 NAL Call. No.: SB599.P45
cDNA cloning and characterization of two barley peroxidase transcripts induced
differentially by the powdery mildew fungus Erysiphe graminis.
Thordal-Christensen, H.; Brandt, J.; Cho, B.H.; Rasmussen, S.K.; Gregersen,
P.L.; Smedegaard-Petersen, V.; Collinge, D.B.
London : Academic Press; 1992 Jun.
Language: English
Descriptors: Hordeum vulgare; Peroxidase; Dna libraries; Erysiphe graminis;
Nucleotide sequences; Amino acid sequences; Gene expression
Abstract: A cDNA library of RNA from barley leaves inoculated with Erysiphe
graminis was screened using labelled cDNA enriched for specific sequences by
subtractive hybridization against RNA from non-inoculated leaves. This
resulted in isolation of several clones representing pathogen induced genes.
By cross-hybridization and sequence analysis, one of the cDNAs (pBT6-3) was
found to be a partial clone representing a putative peroxidase, for which a
full-length cDNA clone (pBH6-301) was subsequently isolated. The predicted
amino acid sequence revealed a 21 amino acid signal peptide and a 294 amino
acid mature protein (31 kDa) and shows 56% amino acid identity to a basic
peroxidase from turnip, 89% to a putative peroxidase from wheat, but only 38%
to the amino acid sequence derived from the cDNA clone (pcD1311) of a second
putative barley peroxidase expressed in leaves. Northern blot analysis showed
that the pBT6-3 (pBH6-301) transcript is elevated as early as 4 h after
inoculation with E. graminis f. sp hordei and that two maxima in transcript
levels appear, which can be correlated with penetration attempts by the
fungus. The amount of the pcD1311 transcript was also found to increase in
inoculated leaves but at a later time point.
32 NAL Call. No.: QK710.P62
cDNA cloning and gene expression of the major prolamins of rice.
Shyur, L.F.; Wen, T.N.; Chen, C.S.
Language: English
Descriptors: Oryza sativa; Structural genes; Dna; Prolamins; Nucleotide
sequences; Amino acid sequences; Peptides; Seed development; Gene expression;
Messenger RNA
Abstract: A full-length cDNA (pS 18) encoding the 16 kDa rice prolamin
composed of 158 amino acids was sequenced. Analysis of N-terminal amino acid
sequence of a major rice prolamin indicated that an 18 amino acid signal
peptide was removed from 16 kDa precursor prolamin to form the 14 kDa prolamin
during seed development. Synthesis of the 16 kDa precursor prolamin began
around 8 days after flowering (DAF), increased remarkably at 8-11 DAF and
gradually reached maximum levels with the maturation of rice seeds.
33 NAL Call. No.: 450 P692
cDNA cloning and sequence analysis of a pathogen-induced thaumatin-like
protein from rice (Oryza sativa).
Language: English
Descriptors: Oryza sativa; Complementary DNA; Cloning; Pathogenesis-related
proteins; Nucleotide sequences; Amino acid sequences; Gene expression; Genetic
regulation; Pseudomonas syringae pv. syringae
34 NAL Call. No.: QK710.P62
cDNA nucleotide sequence and expression of a maize cytoplasmic ribosomal
protein S13 gene.
Language: English
Descriptors: Zea mays; Complementary DNA; Multigene families; Ribosomes;
Proteins; Nucleotide sequences; Amino acid sequences; Cytoplasm; Gene
expression; Transcription; Messenger RNA; Cell differentiation
Abstract: The complete amino acid sequence of a cytoplasmic ribosomal protein
S13 of maize was deduced from the cDNA isolated from a maize cDNA library. The
encoded protein is 151 amino acids long and shows a homology of 73% with the
corresponding protein S13 of rat. Southern blots analysis shows that the maize
protein S13 is encoded by a small multigene family conserved in plant species
closely related to maize. The S13 RNAs accumulate preferentially in
proliferating tissues and cells and their transcription occurs in parallel to
the DNA synthesis.
35 NAL Call. No.: QK710.P62
cDNA nucleotide sequence and expression of a maize cytoplasmic ribosomal
protein S13 gene.
Language: English
Descriptors: Zea mays; Complementary DNA; Multigene families; Ribosomes;
Proteins; Nucleotide sequences; Amino acid sequences; Cytoplasm; Gene
expression; Transcription; Messenger RNA; Cell differentiation
Abstract: The complete amino acid sequence of a cytoplasmic ribosomal protein
S13 of maize was deduced from the cDNA isolated from a maize cDNA library. The
encoded protein is 151 amino acids long and shows a homology of 73% with the
corresponding protein S13 of rat. Southern blots analysis shows that the maize
protein S13 is encoded by a small multigene family conserved in plant species
closely related to maize. The S13 RNAs accumulate preferentially in
proliferating tissues and cells and their transcription occurs in parallel to
the DNA synthesis.
36 NAL Call. No.: 450 AM36
Cell- and tissue-specific expression of rice histone gene transcripts during
anther and pollen development in henbane (Hyoscyamus niger).
Raghavan, V.; Jiang, C.; Bimal, R.
Language: English
Descriptors: Hyoscyamus niger; Anthers; Pollen; Gene expression; Histones;
Hybridization; Transcription; Plant development; Spores; Ultrastructure; Oryza
sativa
Abstract: We have monitored by in situ hybridization the cell- and
tissue-specific expression of a rice histone H3 gene during anther and pollen
development in henbane (Hyoscyamus niger). Autoradiographic silver grains
generated by hybridization of 35S-labeled antisense probe were present in more
or less the same density in all the cells of the anther primordium. During
later development of the anther, there was a sequential accumulation of
histone mRNA beginning in the epidermis on the outside and ending in the
tapetum inside. These changes in transcript abundance in the sporophytic cells
of the anther were also related to the stage of microsporogenesis. Transcript
level increased during sporogenesis and reached a maximum in mature pollen
grains collected from open flowers.
37 NAL Call. No.: 500 N21P
Cell type-preferred expression of maize cab-m1: repression in bundle sheath
cells and enhancement in mesophyll cells.
Bansal, K.C.; Bogorad, L.
Language: English
Descriptors: Zea mays; Chlorophyll a/b binding protein; Gene expression;
Genetic code; Light harvesting complexes; Nucleotide sequences; Photosystem
ii; Transcription
Abstract: Different sets of genes for photosynthesis are expressed in
mesophyll cells (MCs) and bundle sheath cells (BSCs)--the two adjacent but
morphologically and functionally distinct types of photosynthetic cells in
leaves of maize and other C4 plants. For example, light-harvesting chlorophyll
a/b-binding proteins of photosystem II, which are encoded by a family of cab
genes, are 3- to 4-fold more abundant in maize MCs than in BSCs. Each maize
cab gene is different from the others in its relative expression in MCs vs.
BSCs and in its degree of photoresponsiveness. The gene cab-m1 is positively
photoregulated and is highly preferentially expressed in MCs. A 159-bp
sequence in the 5' flanking region of this gene (-1026 to -868 relative to the
translation start site) is required for MC-preferred expression of a reporter
gene in greening maize leaves. Deletion as well as gain-of-function
experiments have now shown that all of the sequence information required for
MC-preferred expression resides within this mesophyll-specifying region and
that cab-m1 is preferentially expressed in MCs because of the presence of two
types of sequence elements: one is required for suppressing expression in BSCs
and the other for promoting expression in MCs. One of the four cis-acting
regions mapped within the mesophyll-specifying region resembles the AT-1 box
of some plant gene negative regulatory elements. Various combinations of such
MC-specific enhancing and BSC-specific repressing regions could make maize cab
gene family members different from one another in their relative expression in
MCs vs. BSCs.
38 NAL Call. No.: S494.5.B563B554
Cell wall metabolism in barley.
Language: English
Descriptors: Hordeum; Cell walls; Cell wall components; Metabolism;
Beta-glucanase; Isoenzymes; Nucleotide sequences; Genetic regulation; Gene
expression; Genetic engineering; Genetic transformation; Malting quality; Seed
germination; Grain; Ultrastructure; Evolution
39 NAL Call. No.: QK710.P62
Cell-type specific expression of three rice genes GOS2, GOS5 and GOS9.
Rey, P.; Diaz, C.; Schilperorrt, R.A.; Hensgens, L.A.M.
Dordrecht : Kluwer Academic Publishers; 1993 Nov.
Plant molecular biology v. 23 (4): p. 889-894; 1993 Nov. Includes references.
Language: English
Descriptors: Oryza sativa; Gene expression; Messenger RNA; Transcription;
Structural genes; Plant proteins; Leaves; Roots; Parenchyma; Photosystem i
Abstract: The cell-type-specific expression of three rice genes, GOS2, GOS5
and GOS9, was studied by mRNA in situ hybridization. Previous northern blot
analysis revealed that these genes were constitutive, green tissue-specific
and root-specific, respectively. In this study, GOS2 transcripts were observed
in all leaf cell types. In roots, a temporal and spatial expression pattern
was noticed. Higher mRNA levels were observed in lateral roots, especially in
parenchymal cells of the vascular cylinder. Expression of GOS5 was mainly
found in chloroplast-containing cells. For GOS9, significant levels of signal
were observed in root and leaf sections.
40 NAL Call. No.: 450 P692
Characterization of a cold-regulated wheat gene related to Arabidopsis cor47.
Guo, W.; Ward, R.W.; Thomashow, M.F.
Language: English
Descriptors: Triticum aestivum; Arabidopsis thaliana; Complementary DNA;
Structural genes; Plant proteins; Nucleotide sequences; Amino acid sequences;
Glycine; Threonine; Histidine; Messenger RNA; Gene expression; Seeds; Genetic
regulation; Cold; Acclimatization; Leaves; Roots; Abscisic acid; Water stress
Abstract: The cDNA clone pWG1 represents a gene, designated cor39, from
Triticum aestivum L. cv Winoka (a winter wheat) that is related to a
cold-regulated Arabidopsis thaliana L. (Heyn) gene, cor47. In vitro
transcription/translation experiments in conjunction with DNA sequence
analysis indicated that cor39 encodes a hydrophilic polypeptide of 39 kD
(isoelectric point of 7.5), designated COR39. The polypeptide is composed
primarily of two sequences, each of which is repeated six times. One sequence,
which is lysine rich, occurs in COR47 (the polypeptide encoded by Arabidopsis
cor47) and group II LEA proteins, polypeptides hypothesized to have roles in
desiccation and drought tolerance). Baker, C. Steele, L. Dure III [1988] Plant
Mol Biol 11: 277-291). The second sequence, which is glycine rich, occurs in
some, but not all, group II LEA proteins. Southern analysis indicated that
wheat has a number of loci related to cor39. Transcripts of about 3.3, 1.5,
and 0.8 kb that hybridize with cor39 were found to accumulate in leaf, root,
and crown tissues of cold-acclimated plants; they accumulated rapidly in
response to low temperature and returned quickly to low levels when plants
were returned to normal growth temperature. Transcripts hybridizing with cor39
were present at relatively high levels in wheat seeds and accumulated in
plants in response to exogenous application of ABA and water stress. The
similarities in expression of wheat and Arabidopsis cor genes and possible
functional relationships among COR39, COR47, and LEA proteins are discussed.
41 NAL Call. No.: QK710.P68
Characterization of the catalase antioxidant defense gene Cat1 of maize, and
its developmentally regulated expression in transgenic tobacco.
Guan, L.; Scandalios, J.G.
Language: English
Descriptors: Nicotiana tabacum; Zea mays; Genome analysis; Clones; Dna;
Nucleotide sequences; Amino acid sequences; Transgenic plants; Gene
expression; Transcription; Beta-glucuronidase; Enzyme activity; Flowering;
Developmental stages
42 NAL Call. No.: QK710.P62
Characterization of the U3 and U6 snRNA genes from wheat: U3 snRNA genes in
monocot plants are transcribed by RNA polymerase III.
Marshallsay, C.; Connelly, S.; Filipowicz, W.
Dordrecht : Kluwer Academic Publishers; 1992 Sep.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 19 (6): p. 973-983; 1992 Sep.
Includes references.
Language: English
Descriptors: Triticum aestivum; Multigene families; Small nuclear RNA;
Ribosomal DNA; Transcription; Gene expression; Rna polymerase; Enzyme
activity; Promoters; Controlling elements; Genetic transformation; Zea mays;
Nucleotide sequences; Direct DNAuptake; Protoplasts; Phylogeny; Molecular
conformation
Abstract: We have demonstrated recently that the genes encoding the U3 small
nuclear RNA (snRNA) in dicot plants are transcribed by RNA polymerase III (pol
III), and not RNA polymerase II (pol II) as in all other organisms studied to
date. The U3 gene was the first example of a gene transcribed by different
polymerases in different organisms. Based on phylogenetic arguments we
proposed that a polymerase specificity change of the U3 snRNA gene promoter
occurred during plant evolution. To map such an event we are examining the U3
gene polymerase specificity in other plant species. We report here the
characterization of a U3 gene from wheat, a monocot plant. This gene contains
the conserved promoter elements, USE and TATA, in a pol III-specific spacing
seen also in a wheat U6 snRNA gene characterized in this report. Both the U3
and the U6 genes possess typical pol III termination signals but lack the cis
element, responsible for 3'-end formation, found in all plant pol II-specific
snRNA genes. In addition, expression of the U3 gene in transfected maize
protoplasts is less sensitive to alpha-amanitin than a pol II-transcribed U2
gene. Based on these data we conclude that the wheat U3 gene is transcribed by
pol III. This observation suggests that the postulated RNA polymerase
specificity switch of the U3 gene took place prior to the divergence of
angiosperm plants into monocots and dicots.
43 NAL Call. No.: QH426.D32
Characterization of two maize HSP90 heat shock protein genes: expression
during heat shock, embryogenesis, and pollen development.
Marrs, K.A.; Casey, E.S.; Capitant, S.A.; Bouchard, R.A.; Dietrich, P.S.;
Mettler, I.J.; Sinibaldi, R.M.
Language: English
Descriptors: Zea mays; Multigene families; Heat shock proteins; Structural
genes; Nucleotide sequences; Amino acid sequences; Promoters; Gene expression;
Genetic regulation; Heat shock; Embryogenesis; Gametogenesis; Pollen; Binding
site; Dna binding proteins; Messenger RNA
Abstract: We have isolated two genes from Zea mays encoding proteins of 82
and 81 kD that are highly homologous to the Drosophila 83-kD heat shock
protein gene and have analyzed the structure and pattern of expression of
these two genes during heat shock and development. Southern blot analysis and
hybrid select translations indicate that the highly homologous hsp82 and hsp81
genes are members of a small multigene family composed of at least two and
perhaps three or more gene family members. The deduced amino acid sequence of
these proteins based on the nucleotide sequence of the coding regions shows
64-88% amino acid homology to other hsp90 family genes from human, yeast,
Drosophila, and Arabidopsis. The promoter regions of both the hsp82 and hsp81
genes contain several heat shock elements (HSEs), which are putative binding
sites for heat shock transcription factor (HSF) commonly found in the
promoters of other heat shock genes. Gene-specific oligonucleotide probes were
synthesized and used to examine the mRNA expression patterns of the hsp81 and
hsp82 genes during heat shock, embryogenesis, and pollen development. The
hsp81 gene is only mildly heat inducible in leaf tissue, but is strongly
expressed in the absence of heat shock during the pre-meiotic and meiotic
prophase stages of pollen development and in embryos, as well as in
heat-shocked embryos and tassels. The hsp82 gene shows strong heat
inducibility at heat-shock temperatures (37-42 degrees C) and in heat shocked
embryos and tassels but is only weakly expressed in the absence of heat shock.
Promoter-GUS reporter gene fusions made and analyzed by transient expression
assays in Black Mexican Sweet (BMS) Maize protoplasts also indicate that the
hsp82 and hsp81 are regulated differentially. The hsp82 promoter confers
strong heat-inducible expression of the GUS reporter gene in heat-treated
cells (60- to 80-fold over control levels), whereas the hsp81 promoter is only
weakly heat inducible (5- to 10-fold over control levels).
44 NAL Call. No.: QH506.E46
Chloroplasts rps15 and the rpoB/C1/C2 gene cluster are strongly transcribed in
ribosome-deficient plastids: evidence for a functioning
non-chloroplast-encoded RNA polymerase.
Hess, W.R.; Prombona, A.; Fieder, B.; Subramanian, A.R.; Borner, T.
Oxford, Eng. : IRL Press; 1993 Feb.
Language: English
Descriptors: Hordeum vulgare; Secale cereale; Transcription; Chloroplasts; Rna
polymerase; Enzyme activity; Ribosomes; Gene expression; Messenger RNA;
Structural genes; Mutants
Abstract: Transcription of plastid genes and transcript accumulation were
investigated in white leaves of the albostrians mutant of barley (Hordeum
vulgare) and in heat-bleached leaves of rye (Secale cereale) as well as in
normal green leaves of both species. Cells of white leaves of the mutant and
cells of heat-bleached leaves bear undifferentiated plastids lacking ribosomes
and, consequently, plastid translation products, among them the subunits of a
putative chloroplast RNA polymerase encoded by the plastid genes rpoA, B, C1
and C2. The following results were obtained. (i) Plastid genes are transcribed
despite the lack of chloroplast gene-encoded RNA polymerase subunits. The
plastid origin of these transcripts was proven. This finding provides evidence
for the existence of a plastid RNA polymerase encoded entirely by nuclear
genes. (ii) Transcripts of the rpo genes and of rps15, but not of genes
involved in photosynthesis and related processes (psbA, rbcL, atpI-H), were
abundantly accumulated in ribosome-deficient plastids. In contrast,
chloroplasts accumulated transcripts of photosynthetic, but not of the rpo
genes. (iii) Differences in transcript accumulation between chloroplasts and
ribosome-deficient plastids are due to different relative transcription rates
and different transcript stability. (iv) The observed differences in
transcription are not caused by an altered pattern of methylation of plastid
DNA. Thus, the prokaryotic plastid genome of higher plants is transcribed by
two RNA polymerases. The observed differences in transcription between
chloroplasts and undifferentiated plastids might reflect different functions
of the two enzymes.
45 NAL Call. No.: QH506.E46
Chloroplasts rps15 and the rpoB/C1/C2 gene cluster are strongly transcribed in
ribosome-deficient plastids: evidence for a functioning
non-chloroplast-encoded RNA polymerase.
Hess, W.R.; Prombona, A.; Fieder, B.; Subramanian, A.R.; Borner, T.
Oxford, Eng. : IRL Press; 1993 Feb.
Language: English
Descriptors: Hordeum vulgare; Secale cereale; Transcription; Chloroplasts; Rna
polymerase; Enzyme activity; Ribosomes; Gene expression; Messenger RNA;
Structural genes; Mutants
Abstract: Transcription of plastid genes and transcript accumulation were
investigated in white leaves of the albostrians mutant of barley (Hordeum
vulgare) and in heat-bleached leaves of rye (Secale cereale) as well as in
normal green leaves of both species. Cells of white leaves of the mutant and
cells of heat-bleached leaves bear undifferentiated plastids lacking ribosomes
and, consequently, plastid translation products, among them the subunits of a
putative chloroplast RNA polymerase encoded by the plastid genes rpoA, B, C1
and C2. The following results were obtained. (i) Plastid genes are transcribed
despite the lack of chloroplast gene-encoded RNA polymerase subunits. The
plastid origin of these transcripts was proven. This finding provides evidence
for the existence of a plastid RNA polymerase encoded entirely by nuclear
genes. (ii) Transcripts of the rpo genes and of rps15, but not of genes
involved in photosynthesis and related processes (psbA, rbcL, atpI-H), were
abundantly accumulated in ribosome-deficient plastids. In contrast,
chloroplasts accumulated transcripts of photosynthetic, but not of the rpo
genes. (iii) Differences in transcript accumulation between chloroplasts and
ribosome-deficient plastids are due to different relative transcription rates
and different transcript stability. (iv) The observed differences in
transcription are not caused by an altered pattern of methylation of plastid
DNA. Thus, the prokaryotic plastid genome of higher plants is transcribed by
two RNA polymerases. The observed differences in transcription between
chloroplasts and undifferentiated plastids might reflect different functions
of the two enzymes.
46 NAL Call. No.: QH301.N32
Circadian control of gene expression and morphogenesis by heat shock in
barley.
Language: English
Descriptors: Hordeum vulgare; Circadian rhythm; Gene expression; Greening;
Heat shock; Morphogenesis; Phytochrome; Messenger RNA
47 NAL Call. No.: QK710.P62
Circadian rhythmicity in the expression of a novel light-regulated rice gene.
Reimmann, C.; Dudler, R.
Language: English
Descriptors: Oryza sativa; Complementary DNA; Structural genes; Plant
proteins; Gene expression; Messenger RNA; Genetic regulation; Circadian
rhythm; Light
Abstract: We have identified and analyzed cDNAs corresponding to a
single-copy gene from rice, designated lir1, whose expression exhibits
dramatic diurnal fluctuations. The cDNAs encode a putative protein of 128
amino acids with no homology to known proteins. Lir1 mRNA accumulates in the
light, reaching maximum and minimum steady-state levels at the end of the
light and dark period, respectively. The oscillations of lir1 mRNA abundance
persist after the plants have been transferred to continuous light or
darkness. Plants germinated in the dark have very low levels of lir1 mRNA,
whereas plants germinated in continuous light express lir1 at an intermediate
but constant level. These results indicate that lir1 expression is controlled
by light and a circadian clock.
48 NAL Call. No.: QK710.P62
The cis-regulatory element CCACGTGG is involved in ABA and water-stress
responses of the maize gene rab28.
Language: English
Descriptors: Zea mays; Genes; Promoters; Controlling elements; Binding site;
Dna binding proteins; Gene expression; Genetic regulation; Abscisic acid;
Water stress; Plant embryos; Leaves
Abstract: The maize gene rab28 has been identified as ABA-inducible in
embryos and vegetative tissues. It is also induced by water stress in young
leaves. The proximal promoter region contains the conserved cis-acting element
CCACGTGG (ABRE) reported for ABA induction in other plant genes. Transient
expression assays in rice protoplasts indicate that a 134 bp fragment (-194 to
-60 containing the ABRE) fused to a truncated cauliflower mosaic virus
promoter (35S) is sufficient to confer ABA-responsiveness upon the GUS
reporter gene. Gel retardation experiments indicate that nuclear proteins from
tissues in which the rab28 gene is expressed can interact specifically with
this 134 bp DNA fragment. Nuclear protein extracts from embryo and
water-stressed leaves generate specific complexes of different electrophoretic
mobility which are stable in the presence of detergent and high salt. However,
by DMS footprinting the same guanine-specific contacts with the ABRE in both
the embryo and leaf binding activities were detected. These results indicate
that the rab28 promoter sequence CCACGTGG is a functional ABA-responsive
element, and suggest that distinct regulatory factors with apparent similar
affinity for the ABRE sequence may be involved in the hormone action during
embryo development and in vegetative tissues subjected to osmotic stress.
49 NAL Call. No.: QH301.N32
Cis-regulatory elements responsible for the tissue-specific expression of the
wheat cab-1 gene.
Language: English
Descriptors: Triticum; Chlorophyll a/b binding protein; Gene expression;
Light; Photosystem ii; Plant proteins
50 NAL Call. No.: 450 P692
Cloning, characterization, and expression of a cDNA encoding a 50-kilodalton
protein specifically induced by cold acclimation in wheat.
Houde, M.; Danyluk, J.; Laliberte, J.F.; Rassart, E.; Dhindsa, R.S.; Sarhan,
F.
Language: English
Descriptors: Triticum aestivum; Cold tolerance; Acclimatization; Protein
synthesis; Induction; Clones; Genetic code; Dna; Gene expression; Genotypes;
Messenger RNA; Genetic variation; Nucleotide sequences; Amino acid sequences
Abstract: We have isolated, sequenced, and expressed a cold-specific cDNA
clone, Wcs120, that specifically hybridizes to a major mRNA species of
approximately 1650 nucleotides from cold-acclimated wheat (Triticum aestivum
L.). The accumulation of this mRNA was induced in less than 24 hours of cold
treatment, and remained at a high steady-state level during the entire period
of cold acclimation in the two freezing-tolerant genotypes of wheat tested.
The expression of Wcs120 was transient in a less-tolerant genotype even though
the genomic organization of the Wcs120 and the relative copy number were the
same in the three genotypes. The mRNA level decreased rapidly during
deacclimation and was not induced by heat shock, drought, or abscisic acid.
The Wcs120 cDNA contains a long open reading frame encoding a protein of 390
amino acids. The encoded protein is boiling stable, highly hydrophilic, and
has a compositional bias for glycine (26.7%), threonine (16.7%), and histidine
(10.8%), although cysteine, phenylalanine, and tryptophan were absent. The
WCS120 protein contains two repeated domains. Domain A has the consensus amino
acid sequence GEKKGVMENIKEKLPGGHGDHQQ, which is repeated 6 times, whereas
domain B has the sequence TGGTYGQQGHTGTT, which is repeated 11 times. The two
domains were also found in barley dehydrins and rice abscisic acid-induced
protein families. The expression of this cDNA in Escherichia coli, using the
T7 RNA polymerase promoter, produced a protein of 50 kilodaltons with an
isoelectric point of 7.3, and this product comigrated with a major protein
synthesized in vivo and in vitro during cold acclimation.
51 NAL Call. No.: QK710.P62
Cloning of cDNA, expression, and chromosomal location of genes encoding the
three types of subunits of the barley tetrameric inhibitor of insect
alpha-amylase.
Language: English
Descriptors: Hordeum vulgare; Complementary DNA; Structural genes; Multigene
families; Enzyme inhibitors; Alpha-amylase; Insects; Nucleotide sequences;
Amino acid sequences; Defense mechanisms; Gene mapping; Gene location;
Chromosomes; Gene expression; Messenger RNA; Endosperm
Abstract: Three cDNA clones from barley developing endosperm, corresponding
to proteins BTAI-CMa, BTAI-CMb and BTAI-CMd, which are the three types of
subunits of the tetrameric inhibitor of insect alpha-amylases, have been
identified and sequenced. The deduced amino acid sequence of BTAI-CMb
corresponds to the CM16/CM17 type of subunit in wheat (92/90% identical
residues) and has one putative N-glycosylation site (NLT) and a possible
kinase-C phosphorylation site (SCR). The BTAI-CMa sequence differs at four
amino acid residues from a previously reported one from cv. Bomi and the
sequence deduced for BTAI-CMd completes (11 N-terminal residues) and confirms
previously available data. The gene for BTAI-CMa (Iat1) is located in the beta
arm of barley chromosome 7H (syn. 1), while genes for both BTAI-CMb (Iat2) and
BTAI-CMd (Iat3) are in the long arm of chromosome 4H. The three genes are
expressed in endosperm and their mRNAS are not detected in the other tissues
tested, except Iat1, which seems to be expressed at a low level in coleoptile
and roots, where it is switched off by 50 micromolars methyl jasmonate.
52 NAL Call. No.: QH442.A1G4
Comparison of barley malt alpha-amylase isozymes 1 and 2: construction of cDNA
hybrids by in vivo recombination and their expression in yeast.
Juge, N.; Sogaard, M.; Chaix, J.C.; Martin-Eauclaire, M.F.; Svensson, B.;
Marchis-Mouren, G.; Guo, X.J.
Language: English
Descriptors: Hordeum vulgare; Saccharomyces cerevisiae; Complementary DNA;
Recombinant DNA; Alpha-amylase; Isoenzymes; Homologous recombination;
Hybrids; Genetic transformation; Gene expression; Secretion; Enzyme activity
Abstract: Germinating barley produces two alpha-amylase isozymes, AMY1 and
AMY2, having 80% amino acid (aa) sequence identity and differing with respect
to a number of functional properties. Recombinant AMY1 (re-AMY1) and AMY2
(re-AMY2) are produced in yeast, but whereas all re-AMY1 is secreted, re-AMY2
accumulates within the cell and only traces are secreted. Expression of
AMY1::AMY2 hybrid cDNAs may provide a means of understanding the difference in
secretion efficiency between the two isozymes. Here, the efficient homologous
recombination system of the yeast, Saccharomyces cerevisiae, was used to
generate hybrids of barley AMY with the N-terminal portion derived from AMY1,
including the signal peptide (SP), and the C-terminal portion from AMY2.
Hybrid cDNAs were thus generated that encode either the SP alone, or the SP
followed by the N-terminal 21, 26, 53, 67 or 90 aa from AMY1 and the
complementary C-terminal sequences from AMY2. Larger amounts of re-AMY are
secreted by hybrids containing, in addition to the SP, 53 or more aa of AMY1.
In contrast, only traces of re-AMY are secreted for hybrids having 26 or fewer
aa of AMY1. In this case, re-AMY hybrid accumulates intracellularly.
Transformants secreting hybrid enzymes also accumulated some re-AMY within the
cell. The AMY1 SP, therefore, does not ensure re-AMY2 secretion and a certain
portion of the N-terminal sequence of AMY1 is required for secretion of a
re-AMY1::AMY2 hybrid.
53 NAL Call. No.: 450 P692
Complementary DNA cloning and sequence analysis of a pathogen-induced putative
peroxidase from rice.
Language: English
Descriptors: Oryza sativa; Complementary DNA; Peroxidase; Nucleotide
sequences; Amino acid sequences; Gene expression; Messenger RNA; Infections;
Pseudomonas syringae pv. syringae
54 NAL Call. No.: 450 P692
Constitutive and inducible aerobic and anaerobic stress proteins in the
Echinochloa complex and rice.
Language: English
Descriptors: Echinochloa; Echinochloa muricata; Echinochloa oryzoides;
Echinochloa crus-galli; Echinochloa crus-pavonis; Oryza sativa; Stress
response; Protein synthesis; Induction; Anaerobic conditions; Aerobic
treatment; Genetic regulation; Gene expression
Abstract: Anaerobic stress resulted in a change in the protein accumulation
patterns in shoots of several Echinochloa (barnyard grass) species and Oryza
sativa (L.) (rice) as resolved by two-dimensional gel electrophoresis. Of the
six Echinochloa species investigated, E. phyllopogon (Stev.) Koss, E. muricata
(Beauv.) Fern, E. oryzoides (Ard.) Fritsch Clayton, and E. crus-galli (L.)
Beauv. are tolerant of anaerobiosis and germinate in the absence of oxygen, as
does rice. In contrast, E. crus-pavonis (H.B.K.) Schult and E. colonum (L.)
Link are intolerant and do not germinate without oxygen. Computer analysis of
the protein patterns from the four tolerant species and rice indicated that
the anaerobic response is of five classes: class 1 proteins, enhanced under
anaerobiosis (9 to 13 polypeptides ranging from 16-68 kD); class 2 proteins,
unique to anaerobiosis (1 to 5 polypeptides ranging from 17-69 kD); class 3
proteins, remained constant under aerobiosis and anaerobiosis; class 4
proteins, prominent only in air and repressed under anoxia (3 to 7
polypeptides ranging from 19-45 kD); and class 5 proteins, unique to
aerobiosis (1 to 4 polypeptides ranging from 18-63 kD). In the intolerant
species, E. colonum and E. crus-pavonis, no polypeptides were enhanced or
repressed under anoxia (class 1 and class 4, respectively), whereas in the
tolerant Echinochloa species and rice, a total of at least 9 to 13 anaerobic
stress proteins and 4 to 7 "aerobic" proteins were noted. Immunoblotting
identified two of the major anaerobic stress proteins as
fructose-1,6-bisphosphate aldolase and pyruvate decarboxylase. Based on the
differential response of the intolerant species to anaerobiosis, we suggest
that another set of genes, whose products may not necessarily be among the
major anaerobic stress polypeptides, might confer tolerance in Echinochloa
under prolonged anaerobic stress.
55 NAL Call. No.: S494.5.B563B554
The control of protein synthesis in developing barley seeds.
Kreis, M.; Shewry, P.R.
Language: English
Descriptors: Hordeum; Plant embryos; Endosperm; Seed development; Genetic
regulation; Protein synthesis; Cereal proteins; Genes; Gene expression;
Nucleotide sequences; Amino acid sequences; Amino acids; Composition; Protein
value; Grain
56 NAL Call. No.: QK710.P62
Coordinate gene expression of five subclass histones and the putative
transcription factors, HBP-1a and HBP-1b, of histone genes in wheat.
Minami, M.; Huh, G.H.; Yang, P.; Iwabuchi, M.
Dordrecht : Kluwer Academic Publishers; 1993 Oct.
Plant molecular biology v. 23 (2): p. 429-434; 1993 Oct. Includes references.
Language: English
Descriptors: Triticum aestivum; Gene expression; Messenger RNA; Histones;
Structural genes; Dna binding proteins; Meristems; Transcription; Seed
germination; Seedling growth
Abstract: The expression of genes encoding five histones (H1,H2A,H2B,H3 and
H4) and the putative transcription factors HBP-1a (17) and HBP-1b (c38) was
examined during early germination and in various tissues of young wheat
seedlings. The steady-state levels of core histone (H2A, H2B, H3 and H4) mRNAs
were coordinately cell cycle-dependent and paralleled the rate of DNA
synthesis during early germination, whereas the expression pattern of the
linker histone (H1) genes differed. The five subclass histone genes were
actively expressed in the meristematic tissues of young seedlings. Moreover,
H1 genes were expressed in leaves that consist mostly of non-proliferating
cells, in which core histone genes showed little expression. Quantitative
alterations to the mRNAs of the putative transcription factors HBP-1a (17) and
HBP-1b (c38) of wheat histone genes were similar to those of the core histone
mRNAs, suggesting that both factors function in the cell cycle-dependent
expression of wheat core histone genes.
57 NAL Call. No.: 450 P692
Coordinate gene response to salt stress in Lophopyrum elongatum.
Gulick, P.J.; Dvorak, J.
Language: English
Descriptors: Gramineae; Elymus elongatus; Gene expression; Genes; Genetic
regulation; Salinity; Sodium chloride; Stress; Roots; Messenger RNA;
Complementary DNA; Nucleotide sequences
Abstract: Lophopyrum elongatum is a highly salt-tolerant relative of wheat. A
previous study showed that the abundance of a number of mRNA species is
enhanced or reduced in the roots of the L. elongatum X Triticum aestivum
amphiploid by salt stress. Eleven genes with enhanced expression in the roots
of salt-stressed L. elongatum plants have been cloned as cDNAS. The clones
were used as probes to characterize temporal expression of these genes in
roots after initiation of salt (250 mm NaCl) stress. All 11 genes are induced
within 2 h after exposure to 250 mm NaCl and reached peak expression after 6
h. The decline of gene expression distinguished two groups, one in which mRNA
concentrations returned to basal levels by 24 h and the other in which this
occurred between 3 and 7 d. One of the 11 clones was found to be homologous to
a multigene family of abscisic acid-induced genes, rab and dhn, identified in
other species. We suggest that the coordinate expression of this large number
of genes reflects the existence of a highly specific early response to salt
stress. We refer to this response as the 'early salt stress response.'
58 NAL Call. No.: QP501.E8
Corn kernel cystein proteinase inhibitor as a novel cystatin superfamily
member of plant origin. Molecular cloning and expression studies.
Abe, M.; Abe, K.; Kuroda, M.; Arai, S.
Language: English
Descriptors: Zea mays; Kernels; Cysteine proteinases; Proteinase inhibitors;
Plant proteins; Genes; Clones; Gene expression; Nucleotide sequences; Amino
acid sequences; Comparisons; Enzyme activity; Inhibition
Abstract: A full-length cDNA clone for a cysteine proteinase inhibitor
(cystatin) was isolated from a lambda gt10 cDNA library of immature corn
kernels by screening with a mixture of cDNA inserts for oryzacystatins I and
II. The cDNA clone spans 960 base pairs, encoding a 135-amino-acid protein
containing a signal peptide fragment. The protein, named corn cystatin 1, is
considered to be a member of the cystatin superfamily, since it contains the
commonly conserved Gln-Val-Val-Ala-Gly region that exists in most known
cystatins as a probable binding site and is significantly similar to other
cystatins in its overall amino acid sequence. Corn cystatin I expressed in
Escherichia coli showed a strong papain-inhibitory activity. Northern blot
analysis showed that the amount of mRNA for corn cystatin I reaches a maximum
2 weeks after flowering and then decreases gradually.
59 NAL Call. No.: 442.8 Z34
Correlation between the size of the intergenic regulatory region, the status
of cytosine methylation of rRNA genes and nucleolar expression in wheat.
Sardana, R.; O'Dell, M.; Flavell, R.
Language: English
Descriptors: Triticum aestivum; Ribosomal DNA; Ribosomal RNA; Loci;
Multigene families; Cytosine; Dna methylation; Nucleolus; Gene expression;
Secondary constrictions; Repetitive DNA; Binding site; Dna binding proteins;
Genetic regulation
Abstract: A large number of wheat rRNA genes are methylated at all the CCGG
sites that are present in the intergenic regions. A smaller number of rRNA
genes are not methylated at one or more CCGG sites. A subset of genes was
found unmethylated at a specific CCGG site just downstream of the array of 135
bp A repeats in the intergenic region. In all the genotypes studied, the rDNA
loci with larger intergenic regions between their genes also possess a greater
number of rRNA genes that are unmethylated at one or more CCGG sites in the
intergenic regions than do the loci with shorter intergenic regions. In four
genotypes (for which data were available), rDNA loci with longer intergenic
regions had larger secondary constrictions on metaphase chromosomes, a measure
of relative locus activity, than the loci with shorter intergenic regions. The
results have been integrated into a model for the control of rDNA expression
based on correlations between cytosine methylation patterns and the number of
upstream 135 bp repeats in intergenic regions. According to this model the 135
bp repeats play a part in the control of gene activity by binding a protein(s)
that is in limiting supply, thereby predisposing the neighbouring gene to
become active preferentially.
60 NAL Call. No.: QK710.P62
Co-transcription pattern of an introgressed operon in the maize chloroplast
genome comprising four ATP synthase subunit genes and the ribosomal rps2.
Stahl, D.J.; Rodermel, S.R.; Bogorad, L.; Subramanian, A.R.
Dordrecht : Kluwer Academic Publishers; 1993 Mar.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (6): p. 1069-1076; 1993 Mar.
Includes references.
Language: English
Descriptors: Zea mays; Transcription; Structural genes;
Adenosinetriphosphatase; Ribosomes; Proteins; Introgression; Chloroplasts;
Genomes; Chloroplast genetics; Gene expression; Messenger RNA; Thylakoids
Abstract: Several examples of the introduction of a gene from one gene
complex into another (introgression) are found when chloroplast RP gene
clusters are compared to those in Escherichia coli or cyanobacteria. Here we
describe the transcript pattern of one such cluster from maize (Zea mays) that
includes the genes for 4 subunits of the thylakoid ATP synthase (atpI, H, F,
61 NAL Call. No.: SB732.6.M65
Cultivar-specific elicitaiton of barley defense reactions by the phytotoxic
peptide NIP1 from Rhynchosporium secalis.
Hahn, M.; Jungling, S.; Knogge, W.
Language: English
Descriptors: Hordeum vulgare; Rhynchosporium secalis; Complementary DNA;
Pathogenesis-related proteins; Nucleotide sequences; Amino acid sequences;
Gene expression; Messenger RNA; Gene location; Alleles; Segregation;
Dominance; Defense mechanisms; Disease resistance; Multigene families; Fungal
diseases; Pathogenicity; Physiological races; Peptides; Mycotoxins; Cultivars;
Genes
62 NAL Call. No.: 450 P692
Cytokinin is required to induce the nitrogen-dependent accumulation of mRNAs
for phosphoenolpyruvate carboxylase and carbonic anhydrase in detached maize
leaves.
Language: English
Descriptors: Zea mays; Gene expression; Messenger RNA; Carbonate dehydratase;
Phosphoenolpyruvate carboxylase; Genetic regulation; Zeatin; Benzyladenine;
Nitrate; Nutrient availability; Leaves; Iaa; Abscisic acid
Abstract: Previous studies with intact maize (Zea mays L.) plants indicated
that phosphoenolpyruvate carboxylase (PEPC) levels are controlled by nitrogen
(N) availability and that this regulation is presumably at the transcriptional
level (B. Sugiharto, K. Miyata, H. Nakamoto, H. Sasakawa, T. Sugiyama [1990]
Plant Physiol 92: 963-969; B. Sugiharto, T. Sugiyama [19921 Plant Physiol 98:
1403-1408). In the present study, detached maize leaves were used to
investigate further the mechanism of N-dependent regulation of gene expression
in C4 plants. PEPC and carbonic anhydrase (CA) mRNA levels decreased in leaves
detached from maize plants. Addition of high nitrate did not prevent this
decrease. However, the addition of zeatin to solutions bathing the cut ends of
the detached leaves inhibited the decrease of PEPC and CA mRNA levels.
Simultaneous addition of high nitrate and zeatin to leaves detached from
N-deficient maize plants caused a large and rapid increase in PEPC and CA mRNA
levels. Zeatin could be replaced by benzyladenine, but not by indoleacetic
acid or abscisic acid. Both CA isozymes were effected and responded in an
identical manner. We conclude that detached maize leaves provide an excellent
experimental system to study the mechanism(s) of N-mediated regulation of PEPC
and CA gene expression. However, zeatin is an essential component of this
system.
63 NAL Call. No.: 450 P692
Cytosolic alkalinization mediated by abscisic acid is necessary, but not
sufficient, for abscisic acid-induced gene expression in barley aleurone
protoplasts.
Language: English
Descriptors: Hordeum vulgare; Gene expression; Messenger RNA; Genes; Genetic
regulation; Abscisic acid; Ph; Alkalinity; Cytosol; Protoplasts; Aleurone
cells
Abstract: We investigated whether intracellular pH (phi) is a causal mediator
in abscisic acid (ABA)-induced gene expression. We measured the change in phi
by a "null-point" method during stimulation of barley (Hordeum vulgare cv
Himalaya) aleurone protoplasts with ABA and found that ABA induces an increase
in pHi from 7.11 to 7.30 within 45 min after stimulation. This increase is
inhibited by plasma membrane H+-ATPase inhibitors, which induce a decrease in
pHi, both in the presence and absence of ABA. This ABA-induced phi increase
precedes the expression of RAB-16 mRNA, as measured by northern analysis.
ABA-induced pHi changes can be bypassed or clamped by addition of either the
weak acids 5,5-dimethyl-2,4-oxazolidinedione and propionic acid, which
decrease the phi, or the weak bases methylamine and ammonia, which increase
the pHi. Artificial phi increases or decreases induced by weak bases or weak
acids, respectively, do not induce RAB-16 mRNA expression. Clamping of the pHi
at a high value with methylamine or ammonia treatment affected the ABA-induced
increase of RAB-16 mRNA only slightly. However, inhibition of the ABA-induced
phi increase with weak acid or proton pump inhibitor treatments strongly
inhibited the ABA-induced RAB-16 mRNA expression. We conclude that, although
the ABA-induced the pHi increase is correlated with and even precedes the
induction of RAB-16 mRNA expression and is an essential component of the
transduction pathway leading from the hormone to gene expression, it is not
sufficient to cause such expression.
64 NAL Call. No.: QK725.P532
Definition and functional implications of gibberellin and abscisic acid
cis-acting hormone response complexes.
Language: English
Descriptors: Hordeum vulgare; Promoters; Alpha-amylase; Controlling elements;
Gibberellic acid; Abscisic acid; Transcription; Gene expression; Genetic
regulation; Nucleotide sequences; Seed development
Abstract: The mechanisms by which cis-acting hormone response elements affect
transcription is unclear. In this study, we demonstrated that a second
"coupling element," identified as O2S, must be present to allow a single copy
of either the gibberellin response element (GARE) or the abscisic acid
response element (ABRE) to mediate their hormonal effects in the barley Amy32b
alpha-amylase gene promoter. The interactive effects of the O2S and the GARE
are constrained positionally and spatially; thus, together they form a
gibberellin response complex (GARC). The absolute requirement of the O2S for
function of the ABRE demonstrates that these together form an abscisic acid
response complex (ABRC). A second copy of the GARE can substitute for the O2S
in the GARC, but only in one orientation. By expressing the GARC-containing
and ABRC-containing promoters in developing aleurone tissue, we showed that
hormonal effects prevent alpha-amylase gene expression during the second half
of grain development, but other mechanisms suppress expression earlier. Our
results suggest that the specific sequence serving as a coupling element in a
given gene promoter will greatly affect where and when the GARE or ABRE will
be able to regulate transcription.
65 NAL Call. No.: QK710.P68
Developmental and pathogen-induced expression of three barley genes encoding
lipid transfer proteins.
Language: English
Descriptors: Hordeum vulgare; Lipoproteins; Gene expression; Genetic code;
Amino acid sequences; Cloning; Dna; Disease resistance; Nucleotide sequences;
Plant diseases
66 NAL Call. No.: 450 P692
Developmental regulation of (1 leads to 3, 1 leads to 4)-beta-glucanase gene
expression in barley: tissue-specific expression of individual isoenzymes.
Slakeski, N.; Fincher, G.B.
Language: English
Descriptors: Hordeum vulgare; Aleurone layer; Scutellum; Leaves; Roots;
Beta-glucanase; Enzyme activity; Regulation; Plant development; Gene
expression; Isoenzymes; Seed germination; Transcription
Abstract: Two genes encode (1 leads to 3,1 leads to 4)-beta-D-glucan
4-glucanohydrolase (EC 3.2.1.73) isoenzymes EI and EII in barley (Hordeum
vulgare L.). Specific DNA probes have been used in Northern analyses to
examine the developmental regulation of individual (1 leads to 3,1 leads to
4)-beta-glucanase genes in the aleurone and scutellum of germinated grain and
in young leaves and young roots. In aleurone and scutella excised from
germinated grain, mRNAs encoding both isoenzymes are present but developmental
patterns differ between the two tissues. Thus, levels of both isoenzyme EI and
EII mRNA increase significantly in the aleurone between 1 and 3 days after the
initiation of germination. In the scutellum, isoenzyme EI mRNA predominates
and decreases as germination proceeds. Isoenzyme EI mRNA appears in young
leaves approximately 8 days after the initiation of germination and levels
rise until about 20 days. Enzyme activity in leaf extracts parallels the
development of isoenzyme EI mRNA. No isoenzyme EII mRNA is detected in the
leaves in this period. Analysis of RNA from different leaf segments indicates
that the isoenzyme EI mRNA is distributed relatively evenly along the length
of the leaf. In young roots, mRNA encoding (1 leads to 3,1 leads to
4)-beta-glucanase isoenzyme EI is detected at high levels 3 to 6 days after
the initiation of germination; again, little or no isoenzyme EII mRNA is
found. Overall, transcription of the (1 leads to 3,1 leads to
4)-beta-glucanase isoenzyme EII gene appears to be restricted to the
germinating grain, whereas isoenzyme EI is expressed in a wider range of
tissues during seedling development.
67 NAL Call. No.: S494.5.B563C87
Developmental regulation of an ABA- and stress-induced protein in barley.
Ho, T.H.D.; Hong, B.; Barg, R.
Language: English
Descriptors: Hordeum vulgare; Gene expression; Messenger RNA; Plant proteins;
Plant embryos; Aleurone layer; Seed development; Genetic regulation; Abscisic
acid; Water stress; Seed germination; Seedling growth; Drought; Cold stress;
Heat shock; Salinity
68 NAL Call. No.: 450 P693
Differences in gene expression between natural and artificially induced leaf
senescence.
Language: English
Descriptors: Hordeum vulgare; Gene expression; Messenger RNA; Complementary
DNA; Leaves; Senescence; Dark; Abscisic acid; Kinetin; Stress; Osmotic
pressure; Abiotic injuries
Abstract: Gene expression during artificially induced senescence of barley
(Hordeum vulgare L.) leaves was examined by in-vitro translation and mRNA
hybridization with several copy-DNA (cDNA) clones for newly induced
transcripts. When detached barley leaves were incubated in darkness,
senescence symptoms as indicated by chlorophyll loss were rapidly induced. By
in-vitro translation, concomitant changes in translatable mRNA levels were
shown to occur with some translation products decreasing and others increasing
in abundance. For closer analysis, cDNA clones for newly induced transcripts
were isolated by differential screening. Six cDNA clones, derived from three
different transcripts were identified and classified according to the
expression of the respective mRNAs. Two of the three transcripts showed very
similar expression patterns: in detached leaves they were induced by abscisic
acid and inhibited by kinetin. They were also induced by wounding and osmotic
stress, but could not be detected in naturally senescing leaves. The third
mRNA, represented by only one of the six cDNA clones, behaved differently.
There was no significant effect of hormone application, wounding or drought
conditions, but the transcript accumulated during natural senescence of barley
flag leaves. We conclude that only a minor part of the mRNA changes observed
during dark incubation of detached leaves is connected with leaf senescence,
whereas stress-related transcripts appear to predominate quantitatively.
69 NAL Call. No.: 442.8 Z8
Differences in the heat-shock response between thermotolerant and
thermosusceptible cultivars of hexaploid wheat.
Weng, J.; Nguyen, H.T.
Language: English
Descriptors: Triticum aestivum; Multigene families; Heat shock proteins; Gene
expression; Messenger RNA; Cultivars; Heat tolerance; Heat; Susceptibility;
Heat shock; Seedlings; Restriction fragment length polymorphism; Genetic
polymorphism; Lines; Heat stress
Abstract: Heat-shock protein (HSP) gene expression in two wheat lines cv
'Mustang' (heat-tolerant) and cv 'Sturdy' (heat-susceptible) were analyzed to
determine if wheat genotypes differing in heat tolerance also differ in
in-vitro HSP synthesis (translatable HSP mRNAs) and steady-state levels of HSP
mRNA. Several sets of mRNA were isolated from seedling leaf tissues which had
been heat-stressed at 37 degrees C for various time intervals. These mRNAs
were hybridized with HSP cDNA or genomic DNA probes (HSP17, 26, 70, 98, and
ubiquitin). Protein profiles were compared using in-vitro translation and 2-D
gels. The Northern slot-blot data from the heat-stress treatment provide
evidence that the heat-tolerant cv 'Mustang' synthesized low molecular weight
(LMW) HSP mRNA earlier during exposure to heat shock and at a higher level
than did the heat-susceptible cv 'Sturdy'. This was especially true for the
chloroplast-localized HSP. The protein profiles shown by 2-D gel analysis
revealed that there were not only quantitative differences of individual HSPs
between the two wheat lines, but also some unique HSPs which were only found
in the 'Mustang' HSP profiles. The high level of RFLP between the two wheat
lines was revealed by Southern blot hybridization utilizing a HSP17 probe.
These data provide a molecular basis for further genetic analysis of the role
of HSP genes in thermal tolerance in wheat.
70 NAL Call. No.: 450 P699
Differential effects of nitrate and light on the expression of glutamine
synthetases and ferredoxin-dependent glutamate synthase in maize.
Sakakibara, H.; Kawabata, S.; Hase, T.; Sugiyama, T.
Kyoto : Japanese Society of Plant Physiologists; 1992 Dec.
Plant and cell physiology v. 33 (8): p. 1193-1198; 1992 Dec. Includes
references.
Language: English
Descriptors: Zea mays; Nitrogen metabolism; Leaves; Glutamate-ammonia ligase;
Enzyme activity; Glutamate synthase; Genetic regulation; Gene expression;
Regulation; Light; Nitrate; Ferredoxin; Photosynthesis; Protein composition
Abstract: The effects of nitrate and light on the expression of genes for
glutamine synthetase (GS) isoproteins and ferredoxin-dependent glutamate
synthase (Fd-GOGAT) were studied in different organs of maize seedlings by
analyzing the levels of the respective polypeptides and mRNAs. In roots, the
levels of plastidic GS and of a novel, root-specific GS molecule localized in
the extraplastidic compartment were increased markedly by nitrate, whereas
Fd-GOGAT and cytosolic GS remained at their initial levels. Ammonia was not
effective in inducing the plastidic GS and Fd-GOGAT but it did induce the
novel GS isoprotein. In leaves, cytosolic and plastidic GSs and Fd-GOGAT were
present in both mesophyll cells (MC) and bundle sheath cells (BSC). Upon
addition of nitrate, the level of plastidic GS increased preferentially in MC,
and upon exposure of etiolated seedlings to light, the levels of plastidic GS
and Fd-GOGAT increased in BSC in a coordinated manner. The relationship
between the expression of genes for GSs and Fd-GOGAT and the physiological
role of the GS/GOGAT cycle is discussed in terms of the characteristics of
nitrogen metabolism in roots, MC, and BSC.
71 NAL Call. No.: SB732.6.M65
Differential expression and induction of chitinases and beta-1,3-glucanases in
response to fungal infection during germination of maize seeds.
Cordero, M.J.; Raventos, D.; San Segundo, B.
St. Paul, MN : APS Press, [c1987-; 1994 Jan.
Molecular plant-microbe interactions : MPMI v. 7 (1): p. 23-31; 1994 Jan.
Includes references.
Language: English
Descriptors: Zea mays; Gibberella fujikuroi; Fungal diseases; Chitinase;
Beta-glucanase; Pathogenesis-related proteins; Seed germination; Gene
expression; Messenger RNA; Coleoptiles; Radicles; Plant embryos
72 NAL Call. No.: QK710.P62
Differential expression of six glutamine synthase genes in Zea mays.
Li, M.G.; Villemur, R.; Hussey, P.J.; Silflow, C.D.; Gantt, J.S.; Snustad,
D.P.
Language: English
Descriptors: Zea mays; Structural genes; Glutamate-ammonia ligase; Gene
expression; Messenger RNA; Plant; Nucleotide sequences; Isoenzymes;
Chloroplasts; Multigene families
Abstract: The maize genome has been shown to contain six glutamine synthetase
(GS) genes with at least four different expression patterns. Noncoding
3'gene-specific probes were constructed from all six GS cDNA clones and used
to examine transcript levels in selected organs by RNA gel blot hybridization
experiments. The transcript of the single putative chloroplastic GS(2) gene
was found to accumulate primarily in green tissues, whereas the transcripts of
the five putative GS(1) genes were shown to accumulate preferentially in
roots. The specific patterns of transcript accumulation were quite distinct
for the five GS(1) genes, with the exception of two closely related genes.
73 NAL Call. No.: 450 P699
Differential expression of the catalase and superoxide dismutase genes in
maize ear shoot tissues.
Language: English
Descriptors: Zea mays; Maize ears; Shoots; Gene expression; Developmental
stages; Catalase; Superoxide dismutase; Enzyme activity; Messenger RNA;
Transcription; Pollination
Abstract: The temporal expression of two major antioxidant gene-enzyme
systems, catalases and superoxide dismutases, has been characterized in the
husk leaf, silk, pistillate flower, whole kernel, and cob of the maize ear
shoot. The catalase activity, CAT-2 and CAT-3 protein levels, and the
steady-state mRNA levels of each of the three Cat genes reveal differential
expression of these transcripts in tissues of the ear shoot. Although Cat1 and
Cat3 expression is observed in all the aforementioned tissues, Cat2 expression
is detected only at the late stages of whole kernel maturation. Because silk
exhibits the same pattern of Cat gene expression as the pericarp, and both
tissues share an identical histological origin, catalase gene expression might
be associated with cell lineage. The levels of total superoxide dismutase
activity and corresponding individual Sod transcripts are fairly constant
throughout the temporal profiles of the ear shoot tissues. However, the degree
of accumulation of the multiple Sod mRNAs in the husk leaf is higher than in
the cob. The possibility that the relative position of a tissue within the ear
shoot influences the degree of accumulation of the various Sod mRNAs is
discussed.
74 NAL Call. No.: QK710.P62
Differential expression of U5snRNA gene variants in maize (Zea mays)
protoplasts.
Language: English
Descriptors: Zea mays; Small nuclear RNA; Ribosomal DNA; Multiple genes;
Multigene families; Controlling elements; Gene expression; Protoplasts;
Genetic transformation; Nucleotide sequences; Genetic variation
Abstract: The small nuclear ribonucleoprotein particles U1, U2, U4/U6 and U5
participate in the removal of introns from pre-messenger RNAs in the nucleus.
Three genes encoding U5snRNAs, the RNA moiety of U5snRNPs, have been isolated
from maize. As in other plant UsnRNA gene families the three maize U5snRNA
genes exhibit sequence variation. Two of the gene variants (MzU5.1 and MzU5.2)
are clearly expressed after transfection into maize leaf protoplasts while the
third gene variant (MzU5.3) is expressed at very low levels. These different
levels of expression cannot be directly correlated with sequence changes in
the highly conserved Upstream Sequence Element (USE) required for expression
of Arabidopsis UsnRNA genes nor with differential stability of the U5snRNA
transcripts. Further sequence elements may therefore have a role in regulating
maize UsnRNA gene expression.
75 NAL Call. No.: 450 P692
Differential induction of distinct glutathione-S-transferases of wheat by
xenobiotics and by pathogen attack.
Language: English
Descriptors: Triticum aestivum; Structural genes; Complementary DNA;
Glutathione transferase; Isoenzymes; Gene transfer; Genetic transformation;
Escherichia coli; Gene expression; Messenger RNA; Genetic regulation;
Erysiphe graminis f.sp. tritici; Erysiphe graminis f.sp. hordei; Puccinia
recondita; Salicylic acid; Cadmium; Herbicides; Glutathione; Enzyme activity
Abstract: We have previously characterized a pathogen-induced gene from wheat
(Triticum aestivum L.) that was named GstA1 based on sequence similarities
with glutathione-S-transferases (GSTs) of maize (R. Dudler, C. Hertig, G.
Rebmann, J. Bull, F. Mauch [1991] Mol Plant Microbe Interact 4:14-18). We have
constructed a full-length GstA1 cDNA by combinatorial polymerase chain
reaction and demonstrate by functional expression of the cDNA in Escherichia
coli that the GstA1-encoded protein has GST activity. An antiserum raised
against a GstA1 fusion protein specifically recognized a protein with an
apparent molecular mass of 29 kD on immunoblots of extracts from bacteria
expressing the GstA1 cDNA and extracts from wheat inoculated with Erysiphe
graminis. The GstA1-encoded protein was named GST29. RNA and immunoblot
analysis showed that GstA1 was only weakly expressed in control plants and was
specifically induced by pathogen attack and by the GST substrate glutathione,
but not by various xenobiotics. In contrast, a structurally and antigenically
unrelated GST with an apparent molecular mass of 25 kD that was detected with
an antiserum raised against GSTs of maize was expressed at a high basal level.
This GST25 and an additional immunoreactive protein named GST26 were strongly
induced by cadmium and by the herbicides atrazine, paraquat, and alachlor, but
not by pathogen attack. Compared with the pathogen-induced GST29, GST25 and
GST26 showed a high affinity toward glutathione-agarose and were much more
active toward the model substrate 1-chloro-2,4-dinitrobenzene. Thus, wheat
contains at least two distinct GST classes that are differentially regulated
by xenobiotics and by pathogen attack and whose members have different enzymic
properties. GST25 and GST26 appear to have a function in xenobiotic
metabolism, whereas GST29 is speculated to fulfill a more specific role in
defense reactions against pathogens.
76 NAL Call. No.: 450 P693
Differential molecular responses to abscisic acid and osmotic stress in
viviparous maize embryos.
Language: English
Descriptors: Zea mays; Plant embryos; Messenger RNA; Gene expression; Genes;
Plant proteins; Embryogenesis; Genetic regulation; Stress; Osmotic pressure;
Abscisic acid; Mutants; Germination; Loci
Abstract: Substantial quantities of mRNA encoding the abundant "Em"
polypeptide accumulate, in planta, in developing embryos of maize (Zea mays
L.). By contrast. accumulation of "Em" mRNA is only barely detectable in
embryos with the vp-5/vp-5 genotype [an abscisic acid (ABA)-deficient
viviparous phenotype]. "Em" mRNA is not detectable within viviparous embryos
of the vp-1/vp-1 genotype that are non-responsive to ABA. Culture of immature
wild-type and vp-5/vp-5 embryos in the presence of exogenous ABA or of an
osmotically active agent prevents precocious germination and results in
expression of the "Em" genes. When vp-1/vp-1 embryos are cultured under
similar conditions, only the application of osmotic stress prevents precocious
germination. However. "Em" mRNA does not accumulate either in ABA-treated or
stressed, arrested embryos, indicating a requirement for ABA perception
through a VP-1-mediated mechanism for "Em" gene expression. Nevertheless.
vp-1/vp-1 embryos do show both ABA and stress responses at the molecular
level. Treatment with ABA causes the accumulation of mRNA encoding a
polypeptide of approx. 30 kDa, whilst osmotic stress induces the accumulation
both of a 30-kDa polypeptide and a set of approx. 20-kDa polypeptides. This
indicates the existence of discrete, parallel ABA and stress response pathways
in developing maize embryos.
77 NAL Call. No.: 450 OS7
Diurnal rhythms of the chlorophyll a/b binding protein mRNAs in wild emmer
wheat and wild barley (Poaceae) in the Fertile Crescent.
Nevo, E.; Meyer, H.; Piechulla, B.
Language: English
Descriptors: Israel; Turkey; Iran; Triticum dicoccoides; Hordeum spontaneum;
Messenger RNA; Chlorophyll a/b binding protein; Circadian rhythm; Gene
expression; Genotypes
78 NAL Call. No.: QK710.P62
DNaseI-sensitive and undermethylated rDNA is preferentially expressed in a
maize hybrid.
Language: English
Descriptors: Zea mays; Ribosomal DNA; Ribosomal RNA; Genes; Dna methylation;
Deoxyribonuclease i; Enzyme activity; Dna modification; Molecular mapping;
Genetic polymorphism; Nucleotide sequences; Nucleolus; Hybrids; Repetitive
DNA; Inbred lines; Gene expression
Abstract: An Eco RI polymorphism, present in the 26S ribosomal RNA gene
(rDNA) of the maize hybrid Sx19 (B73 X Mo17), was utilized to correlate DNaseI
sensitivity, undermethylation and expression in rDNA. We had previously shown
that in double digest experiments with methylation-sensitive restriction
enzymes and Eco RI, Sx19 rDNA fragments originating from repeat units with two
Eco RI sites (8.0 kb) are undermethylated, whereas the fragments originating
from repeat units with a single Eco RI site (9.1 kb) are completely
methylated. In the present study, Sx19 rDNA chromatin structure was examined
by purifying intact nuclei and digesting them briefly with increasing amounts
of DNaseI. Analysis of this DNA with Eco RI showed that the 8.0 kb rDNA
fragments are extremely sensitive to DNaseI digestion, while the 9.1 kb rDNA
fragments are relatively resistant to digestion even at high levels of DNaseI.
Specific sites hypersensitive to DNaseI cleavage were mapped to a region in
the intergenic spacer (IGS) near the major undermethylated site. Analysis of
polymerase chain reaction (PCR) products synthesized using Sx19, B73, and Mo17
DNAs as templates indicated that the Eco RI polymorphism is due to a base
change in the recognition site. Direct rRNA sequencing identified a
single-base change in Mo17 rRNA relative to B73 rRNA. Allele-specific
oligonucleotide probes containing the region surrounding and including the Eco
RI polymorphic site were utilized to detect a nucleolar dominance effect by
quantitating levels of rRNA transcripts in Sx19 and the reciprocal cross.
Results from these single-base-pair mismatch hybridization experiments
indicate that the majority of the rRNA transcripts in Sx19 originate from the
DNaseI-sensitive, undermethylated, Eco RI-polymorphic rDNA repeat units.
79 NAL Call. No.: 500 N21P
Dominant transposition-deficient mutants of maize Activator (Ac) transposase.
Kunze, R.; Behrens, U.; Courage-Franzkowiak, U.; Feldmar, S.; Kuhn, S.;
Lutticke, R.
Language: English
Descriptors: Zea mays; Gene expression; Mutants; Petunia; Transposable
elements; Genetic code; Complementation
Abstract: The maize transposable element Activator (Ac) encodes a transposase
(TPase) protein, whose DNA-binding domain is located in a basic region around
aa 200. The N-terminal 102 aa of the TPase are not required for the
transposition reaction. In transfected petunia protoplasts, we analyzed the
protein levels of the N-terminally truncated TPase and mutants thereof and the
corresponding transposition frequencies. The TPase protein forms large
insoluble aggregates at high expression levels. There is no proportionality
observed between TPase levels and transposition frequency. Twenty-one
mutations (of 26), which are distributed over the whole length of the protein,
inactivate the TPase completely. By coexpressing inactive mutant and active
truncated TPase, it was found that several mutations have a trans-dominant
inhibitory effect. Among those are two DNA-binding-deficient mutants,
indicating that inhibition of the active TPase is not caused by competition
for the binding sites on the transposon. Accordingly, Ac TPase acts as an
oligo- or multimer formed by protein-protein interactions. Peculiarly, two
mutants lacking 53 and 98 aa from the C terminus that are themselves
transpositionally inactive lead to an increased excision frequency when they
are coexpressed with the active truncated TPase.
80 NAL Call. No.: QK710.P62
Dynamical behavior of psb gene transcripts in greening wheat seedlings. I.
Time course of accumulation of the psbA through psbN gene transcripts during
light-induced greening.
Language: English
Descriptors: Triticum aestivum; Structural genes; Plant proteins; Photosystem
ii; Gene expression; Messenger RNA; Greening; Seedlings; Transcription;
Genetic regulation; Light; Plastids; Chloroplast genetics
Abstract: The time course of the accumulation of the transcripts from 13 psb
genes encoding a major part of the proteins composing photosystem II during
light-induced greening of dark-grown wheat seedlings was examined focusing on
early stages of plastid development (0.5 h through 72 h). The 13 genes can be
divided into three groups. (1) The psbA gene is transcribed as a single
transcript of 1.3 kb in the dark-grown seedlings, but its level increases 5-
to 7-fold in response to light due to selective increase in RNA stability as
well as in transcription activity. (2) The psbE-F-L-J operon, psbM and psbN
genes are transcribed as a single transcript of 1.1 kb, two transcripts of 0.5
and 0.7 kb and a single transcript of 0.3 kb, respectively, in the dark-grown
seedlings. The levels of accumulation of every transcript remain unchanged or
rather decrease during plastid development under illumination. (3) The
psbK-I-D-C gene cluster and psbB-H operon exhibit fairly complicated northern
hybridization patterns during the greening process. When a psbC or psbD gene
probe was used for northern hybridization, five transcripts differing in
length were detected in the etioplasts from 5-day old dark-grown seedlings.
After 2 h illumination, two new transcripts of different length appeared.
Light induction of new transcripts was also observed in the psbB-H operon.
81 NAL Call. No.: QK725.P54
The effect of different promoter-sequences on transient expression of gus
reporter gene in cultured barley (Hordeum vulgare L.) cells.
Chibbar, R.N.; Kartha, K.K.; Datla, R.S.S.; Leung, N.; Caswell, K.; Mallard,
C.S.; Steinhauer, L.
Language: English
Descriptors: Hordeum vulgare; Genetic transformation; Promoters; Structural
genes; Introns; Actin; Alcohol dehydrogenase; Cauliflower mosaic caulimovirus;
Recombinant DNA; Reporter genes; Beta-glucuronidase; Gene expression;
Transgenic plants; Laboratory methods
Abstract: The cauliflower mosaic virus 35S (35S) and the enhanced 35S (E35S)
promoters fused with maize alcoholdehydrogenase (Adh1) intron1 or maize
shrunken locus (sh1) intron1 along with maize Adh1 and rice actin (Act1)
promoters fused to their respective first introns were tested for transient
expression of the E.coli beta- glucuronidase (gus) reporter gene in cultured
barley (Hordeum vulgare L) cells. The plasmids, carrying the respective
promoter- intron combinations to drive the gus fused to nopaline synthase
(nos) terminator, were introduced into cultured barley cells using a particle
gun. The rice Act1 promoter with its first intron gave the highest expression
of all promoter intron combinations studied. This was followed by the E35S
promoter and no significant differences were observed between the other two
promoters tested. The rice actin promoter is now being used to drive
selectable marker genes to obtain stably transformed cereal cells.
82 NAL Call. No.: 450 P692
The effect of heat shock on morphogenesis in barley. Coordinated circadian
regulation of mRNA levels for light-regulated genes and of the capacity for
accumulation of chlorophyll protein complexes.
Beator, J.; Potter, E.; Kloppstech, K.
Language: English
Descriptors: Hordeum vulgare; Gene expression; Messenger RNA; Chlorophyll a/b
binding protein; Ribulose-bisphosphate carboxylase; Plastocyanins; Structural
genes; Heat shock; Circadian rhythm; Plant proteins; Genetic regulation;
Greening; Chlorophyll; Heat shock proteins; Ubiquitin
Abstract: The effect of daily heat-shock treatments on gene expression and
morphogenesis of etiolated barley (Hordeum vulgare) was investigated.
Heat-shock treatments in the dark induced shortening of the primary leaves and
the coleoptiles to the length of those in light-grown plantlets. In addition,
the mRNA levels of the light-induced genes that were investigated were raised
under these conditions and showed distinct oscillations over a period of at
least 3 d. While the mRNA levels for chlorophyll alb binding protein (LHC II),
plastocyanin, and the small subunit of ribulose-1,5-bisphosphate carboxylase
had maxima between 8 and 12 Pm (12-16 h after the last heat-shock treatment),
the mRNA levels for thionin oscillated with a phase opposed to that of LHC II.
Etiolated barley, the circadian oscillator of which was synchronized by cyclic
heat-shock treatments, was illuminated for a constant interval at different
times of the day; this led to the finding that greening was fastest at the
time when the maximal levels of mRNA for LHC II were also observed. Whereas
accumulation of chlorophyll a during a 4-h period of illumination oscillated
by a factor of 3, chlorophyll b accumulation changed 10- to 15-fold.
Similarly, accumulation of LHC II was highest when pigments accumulated
maximally. Hence, greening or, in other words, thylakoid membrane assembly is
under control of the circadian oscillator. expression and morphogenesis of
etiolated barley (Hordeum vulgare) was investigated. Heat-shock treatments in
the dark induced shortening of the primary leaves and the coleoptiles to the
length of those in light-grown plantlets. In addition, the mRNA levels of the
light-induced genes that were investigated were raised under these conditions
and showed distinct oscillations over a period of at least 3 d. While the mRNA
levels for chlorophyll alb binding protein (LHC II), plastocyanin, and the
small subunit of ribulose-1,5-bisphosphate carboxylase had maxima between 8
and 12 PM (12-16 h after the last heat-shock treatment), the mRNA levels for
thionin oscillated with a phase opposed to that of LHC II. Etiolated barley,
the circadian oscillator of which was synchronized by cyclic heat-shock
treatments, was illuminated for a constant interval at different times of the
day; this led to the finding that greening was fastest at the time when the
maximal levels of mRNA for LHC II were also observed. Whereas accumulation of
chlorophyll a during a 4-h period of illumination oscillated by a factor of 3,
chlorophyll b accumulation changed 10- to 15-fold. Similarly, accumulation of
LHC II was highest when pigments accumulated maximally. Hence, greening or, in
other words, thylakoid membrane assembly is under control of the circadian
oscillator.
83 NAL Call. No.: QK745.J6
Effects of abscisic acid analogues on abscisic acid-induced gene expression in
barley aleurone protoplasts: relationship between structure and function of
the abscisic acid molecule.
Language: English
Descriptors: Hordeum vulgare; Protoplasts; Gene expression; Induction;
Abscisic acid; Analogs; Molecular conformation; Binding site; Chemical
reactions
Abstract: A 520 The plant hormone abscisic acid (ABA) mediates gene
expression in barley aleurone protoplasts. In order to elucidate the essential
functional groups of the ABA molecule, the specificity of a number of ABA
analogues for inducing ABA-regulated gene (e.g., RAB, BASI) expression in
barley aleurone protoplasts was studied. These analogues have modifications at
three different positions of the ABA molecule: (a) the 1'-hydroxyl group
(1'-deoxy ABA), (b) the carboxyl group (ABA-methyl ester or ABA-glucose
ester), and (c) both the 1'-hydroxyl and 4'-carbonyl groups (alpha-ionylidene
acetic acid). The importance of the different putative functional groups was
analyzed. The dose-response analysis of ABA analogues upon the induction gene
expression showed the following order: ABA > ABA methyl ester > 1'-deoxy ABA >
ABA glucose ester > alpha-ionylidene acetic acid > alpha-beta-ionone.
84 NAL Call. No.: S494.5.B563C87
Effects of abscisic acid and abscisic acid analogues on intracellular calcium
level and gene expression in barley aleurone protoplasts.
Wang, M.; Duijn, B. van; Meulen, R.M. van der; Heidekamp, F.
Dordrecht : Kluwer Academic Publishers; 1992.
Current plant science and biotechnology in agriculture v. 13: p. 635-642;
1992. In the series analytic: Progress in plant growth regulation / edited by
C.M. Karssen, L.C. Van Loon and D. Vreugdenhil. Proceedings of the 14th
International Conference on Plant Growth Substances held July 21-26, 1991,
Amsterdam, Netherlands. Includes references.
Language: English
Descriptors: Hordeum vulgare; Abscisic acid; Analogs; Ketones; Calcium ions;
Aleurone layer; Protoplasts; Gene expression; Messenger RNA; Structural
genes; Plant proteins
85 NAL Call. No.: 450 P699
Elevated levels of tubulin transcripts accompany the GA3-induced elongation of
oat internode segments.
Language: English
Descriptors: Avena sativa; Cell growth; Gene expression; Gibberellic acid;
Internodes; Transcription
Abstract: Plant cell elongation involves the deposition of nascent cellulose
microfibrils, the orientation of which is regulated in part by the cortical
microtubule array. To determine whether changes in tubulin gene expression are
associated with cell elongation, we examined GA3-elicited growth of excised
internode segments of Avena sativa. Internode elongation was barely detectable
after 6 h of GA3 treatment, when levels of beta-tubulin transcripts had
increased 5-6 fold over levels found in untreated controls. Elongation
continued for 48 h, whereas tubulin transcript levels reached a peak at 24 h
and then declined. The extent of internode elongation and the level of tubulin
transcript accumulation were dependent upon both concentration and duration of
GA3 treatment. Although a 1 h pulse of GA3 treatment was sufficient to induce
elongation and enhance tubulin transcript levels, constant GA3 application was
necessary to elicit the maximum growth and transcript accumulation responses.
Inhibition of internode elongation by abscisic acid and
2,6,dichlorobenzonitrile (an inhibitor of cellulose biosynthesis) or
cycloheximide inhibited the GA3-mediated growth response and the accompanying
elevation of tubulin transcript levels. The strong correlation we observed
between internode elongation and tubulin transcript level suggests that
tubulin gene expression is regulated in close association with cell
elongation.
86 NAL Call. No.: S494.5.B563C87
The endosperm-specific activity of a rice prolamin promoter in transgenic
tobacco.
Language: English
Descriptors: Oryza sativa; Nicotiana tabacum; Promoters; Prolamins;
Recombinant DNA; Reporter genes; Beta-glucuronidase; Gene expression;
Histoenzymology; Endosperm
87 NAL Call. No.: QK725.P54
Enhanced GUS gene expression in cereal/grass cell suspensions and immature
embryos using the maize ubiquitin-based plasmid pAHC25.
Taylor, M.G.; Vasil, V.; Vasil, I.K.
Language: English
Descriptors: Triticum aestivum; Zea mays; Pennisetum Americanum; Saccharum
officinarum; Pennisetum purpureum; Panicum maximum; Genetic transformation;
Transgenic plants; Plasmid vectors; Direct DNAuptake; Ubiquitin; Promoters;
Recombinant DNA; Reporter genes; Beta-glucuronidase; Gene expression; Cell
suspensions
Abstract: Transient GUS (beta-glucuronidase) expression was visualized in
cell suspensions of Triticum aestivum, Zea mays, Pennisetum glaucum, Saccharum
officinarum, Pennisetum purpureum and Panicum maximum after microprojectile
bombardment with pBARGUS and pAHC25 plasmid DNAs. pBARGUS contains the GUS
(UidA) gene coding region driven by the Adh1 promoter and the Adh1 intron 1,
as well as the BAR gene coding region driven by the CaMV 35S promoter and the
Adh1 intron 1. pAHC25 contains the GUS and BAR gene coding regions driven by
the maize ubiquitin promoter, first exon and first intron (Ubi1). The
effectiveness of the constructs was first compared in cell suspension cultures
by counting blue expression units (b.e.u.). The expression of construct pAHC25
ranged from 3 to 50 fold greater than pBARGUS in different species. In
addition, the two plasmids were quantitatively compared in Triticum aestivum
and Zea mays by using the more sensitive GUS fluorometric assay to determine
the amount of methylumbellyferride (MU) produced. There was more than a 30
fold increase in MU production with pAHC25 than with pBARGUS in the wheat
suspension, while the maize suspension showed only a 2.5 fold increase with
the pAHC25 construct. Transient GUS expression was also visualized in immature
embryos of Pennisetum glaucum following bombardment with pBARGUS and pAHC25
DNA. Expression of plasmid pAHC25 was twice as high as pBARGUS. A comparison
of two DNA/gold preparation methods, as well as repeated sonications of the
DNA/gold mixture, had no effect on the number of b.e.u.
88 NAL Call. No.: 381 J824
Evidence for the translational control of storage protein gene expression in
oat seeds.
Language: English
Descriptors: Avena sativa; Seeds; Plant proteins; Genes; Gene expression;
Translation; Protein synthesis; Genetic regulation; Avenin; Globulins
Abstract: We employed a rapid fractionation method coupled with a sensitive
enzyme-linked immunosorbent assay to quantify the globulins and avenins in
developing and mature oat seeds. On a molar basis, there is approximately
10-11 times as much globulin as avenin. Pulse labeling of endosperm proteins
indicated that the rate of globulin synthesis is approximately nine times that
of avenin. In addition, neither protein class showed any signs of degradation
during this experiment. Analysis of the storage protein mRNAs indicates that
both globulin and avenin transcripts are associated with membrane-bound
polysomes and are found in similar concentrations within the membrane-bound
polysome fraction. We found that avenin and globulin mRNAs are fully loaded
with ribosomes, suggesting that initiation is not rate-limiting for
translation of either protein. Rates of globulin and avenin synthesis were
similar when synthetic storage protein mRNAs were translated in vitro.
Translation of equimolar amounts of globulin and avenin mRNAs in the same
reaction showed equivalent amounts of protein synthesized when compared with
globulin and avenin mRNAs translated in separate reaction mixes. We propose
that translation elongation or termination reactions are likely regulatory
steps for controlling storage protein synthesis in oat endosperm.
89 NAL Call. No.: 450 P692
Expression in Escherichia coli of cytochrome c reductase activity from a maize
NADH:nitrate reductase complementary DNA.
Campbell, W.H.
Language: English
Descriptors: Zea mays; Nadh; Nitrate reductase; Dna; Gene expression;
Escherichia coli; Nadh dehydrogenase; Enzyme activity; Clones; Amino acid
sequences
Abstract: A cDNA clone was isolated from a maize (Zea mays L. cv W64A X
WL83E) scutellum lambda gt11 library using maize leaf NADH:nitrate reductase
Zmnr1 cDNA clone as a hybridization probe; it was designated Zmnr1S. Zmnr1S
was shown to be an NADH:nitrate reductase clone by nucleotide sequencing and
comparison of its deduced amino acid sequence to Zmnr1. Zmnr1S, which is 1.8
kilobases in length and contains the code for both the cytochrome b and flavin
adenine dinucleotide domains of nitrate reductase, was cloned into the EcoRI
site of the Escherichia coli expression vector pET5b and expressed. The cell
lysate contained NADH:cytochrome c reductase activity, which is a
characteristic partial activity of NADH:nitrate reductase dependent on the
cytochrome b and flavin adenine dinucleotide domains. Recombinant cytochrome c
reductase was purified by immunoaffinity chromatography on monoclonal antibody
Zm2(69) Sepharose. The purified cytochrome c reductase, which had a major size
of 43 kilodaltons, was inhibited by polyclonal antibodies for maize leaf
NADH:nitrate reductase and bound these antibodies when blotted to
nitrocellulose. Ultraviolet and visible spectra of oxidized and NADH-reduced
recombinant cytochrome c reductase were nearly identical with those of maize
leaf NADH:nitrate reductase. These two enzyme forms also had very similar
kinetic properties with respect to NADH-dependent cytochrome c and
ferricyanide reduction.
90 NAL Call. No.: QK710.P62
Expression of a cystein proteinase inhibitor (oryzacystatin-I) in transgenic
tobacco plants.
Language: English
Descriptors: Oryza sativa; Nicotiana tabacum; Complementary DNA; Proteinase
inhibitors; Cysteine proteinases; Recombinant DNA; Transgenics; Genetic
transformation; Gene expression; Genetic resistance; Pest resistance; Leaves;
Roots; Seeds
Abstract: Expression of cysteine proteinase inhibitors (cystatins) in tobacco
or other plants has the potential for improving resistance against pathogens
and insects that possess cysteine proteinases. A chimeric gene containing a
cDNA clone of rice cystatin (oryzacystatin-I; OC-I), the caulifower mosaic
virus 35S promoter, and the nopaline synthase 3' region was introduced into
tobacco plants by Agrobacterium tumefaciens. The presence of the chimeric gene
in transgenic plants was detected by a polymerase chain reaction-amplified
assay, and transcriptional activity was shown by RNA blot analysis. Heated
extracts from transgenic tobacco plants, as well as from progeny which were
obtained by selfing a primary transformant, contained protein bands that
corresponded in molecular mass to OC-I and reacted with antibodies raised
against rOC, a recombinant OC-I protein produced by Escherichia coli. Similar
bands were absent in extracts from untransformed control plants. OC-I levels
reached 0.5% and 0.6% of the total soluble proteins in leaves and roots,
respectively, of some progeny. On a fresh weight basis, the OC-I content was
higher in leaves (50 micrograms/g) than in roots (30 micrograms/g). OC-I was
partially purified from protein extracts of rice seeds and from transgenic
tobacco leaves by affinity to anti-rOC antibodies. OC-I from both sources was
active against papain.
91 NAL Call. No.: 450 P699
Expression of a gene specific for iron deficiency (Ids3) in the roots of
Hordeum vulgare.
Language: English
Descriptors: Hordeum vulgare; Roots; Iron; Nutrient deficiencies; Genetic
regulation; Gene expression; Chelating agents; Biosynthesis; Metabolism; Ion
transport; Siderophores; Genetic code; Biochemical pathways; Nucleotide
sequences; Amino acid sequences
Abstract: To clone genes required for the synthesis of mugineic acid (MA) or
for the transport of Fe(III)-MA, a lambda ZAPII cDNA library was constructed
from poly(A)+-RNA isolated from Fe-deficient barley roots. The cDNA library
was then used for differential screening of barley roots that had been grown
in the presence and absence of iron. Seven clones that hybridized specifically
to the probe for Fe deficiency were selected. One clone, presumably encoding a
full-length mRNA, as deduced from Northern hybridization, was sequenced. The
clone consisting of 1685 nucleotides encoded a putative protein of 169 amino
acids and an Mr of 18704. The gene was specifically expressed in the roots of
iron-deficient barley. A search for homologies in a protein database (NBRF)
revealed that the predicted protein product has a functional peptide domain
that resembles that of 2-oxoglutarate-dependent dioxygenases.
92 NAL Call. No.: 450 P692
Expression of a maize ubiquitin gene promoter-bar chimeric gene in transgenic
rice plants.
Language: English
Descriptors: Oryza sativa; Promoters; Introns; Exons; Structural genes;
Ubiquitin; Recombinant DNA; Reporter genes; Marker genes; Acyltransferases;
Genetic transformation; Direct DNAuptake; Electroporation; Transgenic plants;
Bilanafos; Herbicide resistance; Streptomyces; Gene expression; Callus;
Regenerative ability
Abstract: We have constructed a chimeric gene consisting of the promoter,
first exon, and first intron of a maize ubiquitin gene (Ubi-1) and the coding
sequence of the bar gene from Streptomyces hygroscopicus. This construct was
transferred into rice (Oryza sativa L.) protoplasts via electroporation, and
10 plants were regenerated from calli that had been selected for resistance to
exogenously supplied bialaphos. Transgenic plants grown in a greenhouse were
resistant to both bialaphos and phosphinothricine at a dosage lethal to
untransformed control plants. Evidence of stable integration of the
transferred gene into the genome of the regenerated primary transformant
plants was obtained from Southern blot analysis. In addition, northern blot
analysis indicated expression and proper splicing of the maize ubiquitin gene
first intron from the primary chimeric transcript in these transgenic rice
plants, and western blot analysis and enzymic assays verified expression of
the active bar gene product. Apparent mendelian segregation for bialaphos
resistance in T1 progeny of primary transformants was confirmed.
93 NAL Call. No.: QK725.P532
Expression of a rice homeobox gene causes altered morphology of transgenic
plants.
Language: English
Descriptors: Oryza sativa; Arabidopsis thaliana; Dna binding proteins;
Structural genes; Genetic transformation; Transgenic plants; Complementary
DNA; Exons; Nucleotide sequences; Amino acid sequences; Molecular mapping;
Restriction fragment length polymorphism; Introns; Leaves; Morphogenesis;
Plant morphology; Gene expression; Messenger RNA; Shoot meristems; Leaf
primordia; Abnormal development
Abstract: We have isolated a cDNA clone encoding a homeobox sequence from
rice. DNA sequence analysis of this clone, which was designated as Oryza
sativa homeobox 1 (OSH1), and a genomic clone encoding the OSH1 sequence have
shown that the OSH1 gene consists of five exons and encodes a polypeptide of
361 amino acid residues. Restriction fragment length polymorphism analysis has
shown that OSH1 is a single-copy gene located near the phytochrome gene on
chromosome 3. Introduction of the cloned OSH1 gene into rice resulted in
altered leaf morphology, which was similar to that of the maize morphological
mutant Knotted-1 (Kn1), indicating that OSH1 is a rice gene homologous to the
maize Kn1 gene. RNA gel blot analysis has shown that the gene is primarily
expressed in the shoot apices of young rice seedlings. This finding is
supported by results of transformation experiments in which the 5' flanking
region of the gene directed expression of a reporter gene in the shoot apex,
particularly in stipules, of transgenic Arabidopsis. To elucidate the
biological function of the OSH1 gene product, the coding region was introduced
into Arabidopsis under the control of the cauliflower mosaic virus 35S
promoter. Almost all transformants showed abnormal morphology. The typical
phenotype was the formation of clumps of abundant vegetative and reproductive
shoot apices containing meristems and leaf primordia, which did not form
elongated shoots. Some transformants with a less severe phenotype formed
elongated shoots but had abnormally shaped leaves and flowers with stunted
sepals, petals, and stamens. The abnormal phenotypes were inherited, and the
level of expression of the introduced OSH1 correlates with the severity of the
phenotype. These findings indicate that the abnormal morphologies of the
transgenic plants are caused by the expression of the OSH1 gene product and,
therefore, that OSH1 is related to the plant development process.
94 NAL Call. No.: S494.5.B563C87
Expression of a rice sulfur-rich 10kDa prolamin gene in E. coli.
Xu, X.M.; Fan, Y.; Yu, M.M.
Language: English
Descriptors: Oryza sativa; Escherichia coli; Structural genes; Lamins; Gene
transfer; Genetic transformation; Gene expression; Nucleotide sequences;
Recombinant DNA; Promoters; Reporter genes; Beta-galactosidase
95 NAL Call. No.: 442.8 Z8
Expression of A/B zeins in single and double maize endosperm mutants.
Paulis, J.W.; Bietz, J.A.; Bogyo, T.P.; Nelsen, T.C.; Darrah, L.L.; Zuber,
M.S.
Language: English
Descriptors: Zea mays; Mutants; Epistasis; Structural genes; Zein; Prolamins;
Endosperm; Opaque-2 maize; Gene expression; Hplc
Abstract: Zeins, the major endosperm proteins in maize (Zea mays L.), are
deficient in the essential amino acids lysine and tryptophan. Some mutant
genes, like opaque-2 (o2) and floury-2 (fl2), reduce the levels of A- and
B-zeins, thereby improving maize's nutritional value. Other mutants, such as
amylose-extender (ae), floury-1 (fl1), soft starch (h), dull-1 (du),
shrunken-1 (sh1), sugary-1 (su1), sugary-2 (su2), and waxy (wx), primarily
affect starch composition, but also alter zein composition. We undertook this
study to examine the effects of some of these mutant genes on A/B-zein
composition and to study the interactions of these genes in double-mutant
combinations. Endosperm prolamins were extracted from inbred B37, ten
near-isogenic single mutants (ae, du, fl1, fl2, h, o2, sh1, su1, su2, and wx),
and most double-mutant combinations. Zeins in these extracts were fractionated
by reversed-phase high-performance liquid chromatography (RP-HPLC) into 22-24
peaks. Of the resulting 22 major peaks the areas of 16 (per milligram
endosperm) were significantly affected by individual mutant genes relative to
the zein composition of the normal inbred. In combination these genes
exhibited significant epistatic interactions in regulating the expression of
individual A/B zeins. Epistatic interactions were judged to be significant
when the amount of a peak in a double mutant differed from the averages for
the peak in the two respective single mutants. The o2 gene, alone and in
combination with other mutant genes, significantly decreased the amounts of
many individual zeins. The effect of the o2 gene was the greatest of all the
genes examined. Various clustering techniques were used to see if mutant
effects could be grouped; among these was principal component analysis, a
multivariate statistical technique that analyzes all peak sizes
simultaneously. Three-dimensional scatter graphs were constructed based on the
first three principal components. For the single mutants, these showed no
relations to gene actions; for the double mutants, however, this technique
showed that four single mutants, o2, sh1, su1 and su2, had the greatest
effects on sein composition when combined with each other and with the
remaining six single mutants.
96 NAL Call. No.: 442.8 Z8
Expression of chalcone synthase, dihydroflavonol reductase, and
flavanone-3-hydroxylase in mutants of barley deficient in anthocyanin and
proanthocyanidin biosynthesis.
Language: English
Descriptors: Hordeum vulgare; Mutants; Mutations; Structural genes;
Controlling elements; Naringenin-chalcone synthase; Oxygenases;
Oxidoreductases; Gene expression; Transcription; Messenger RNA; Dna; Dna
probes; Dna binding proteins; Anthocyanins; Biosynthesis; Nucleotide
sequences; Amino acid sequences; Restriction mapping
Abstract: A barley (cv Triumph) cDNA library was screened with a cDNA probe
encoding flavanone-3-hydroxylase of Antirrhinum majus. A full-length clone
coding for a protein of 377 amino acids (42 kDa), with an overall homology of
71% and a central domain homology of 85% to the Antirrhinum protein, was
isolated. This novel barley cDNA and two previously isolated cDNAs encoding
chalcone synthase and dihydroquercetin reductase, respectively, were used to
study the transcription of the corresponding genes in testa pericarp tissue
from ant 13 mutants of barley. No or very low levels of transcripts are found
in mutants ant 13-152, ant 13-351, and ant 13-353. It is concluded that the
gene Ant 13 encodes a transcription factor operating in the flavonoid
biosynthesis of barley. Transcription of the gene for the
flavanone-3-hydroxylase (subunit) was also studied in an ant 17 mutant of
barley. Mutant ant 17-352 transcribes the gene at normal or elevated levels.
The mutant is blocked in the synthesis of dihydroquercetin and accumulates
derivatives of eriodictyol, the precursor of dihydroquercetin. The combined
observations suggest that Ant 17 is the structural gene for a barley
flavanone-3-hydroxylase subunit, and that the mutant allele is a mutation in
the structural domain of the gene.
97 NAL Call. No.: 450 P692
Expression of chloroplast and mitochondrial genes during microsporogenesis in
maize.
Language: English
Descriptors: Zea mays; Mitochondria; Chloroplasts; Gene expression; Pollen;
Ontogeny; Developmental stages; Transcription; Mitosis; Plastids
Abstract: Mitochondrial and plastid gene expression has been examined during
maize (Zea mays) microsporogenesis. Accumulation of transcripts was found for
three mitochondrial genes studied (cob, atp6, and atp9) at the mid-term of
pollen development. In contrast, these mitochondrial transcripts were
undetectable in mature pollen. Southern and DNA gel blot experiments showed
that the copy number of mitochondrial genes was amplified in microspores at
stages preceding the accumulation of these transcripts. Plastid transcripts of
the photosynthetic psbA and rbcL genes could not be detected after the two
mitoses, whereas precursors of the 16S rRNA are detected at low levels.
98 NAL Call. No.: QK710.P62
Expression of heat shock proteins during development of barley.
Kruse, E.; Liu, Z.; Kloppstech, K.
Language: English
Descriptors: Hordeum vulgare; Heat shock proteins; Precursors; Multigene
families; Gene expression; Messenger RNA; Seedlings; Seedling stage; Leaves;
Genetic regulation; Heat shock; Plastids; Crop growth stage; Amino acid
sequences
Abstract: Barley heat shock proteins have been cloned, characterized by
hybrid release translation Clones coding for proteins of 17, 18, 30, 32 and 70
kDa have been obtained. Out of these the 32 and 30 kDa proteins have been
characterized as precursors to plastidic proteins of 26 kDa by
posttranslational transport and by cDNA sequencing. The coding regions of
these two transcribed genes are highly homologous. Accumulation of the plastid
HSP as well as of HSP 70 as well as their corresponding mRNAs has been studied
in 2- to 6-day old seedlings and in the 7-day old barley leaf. The mRNA for
all investigated proteins were only found after a heat shock; the mRNA levels
increase towards the tip of the leaf and with development. Furthermore, under
the conditions used the mRNAs for all investigated heat shock proteins
accumulate in parallel. Unexpectedly, both proteins, HSP 70 and HSP 26, are
found by western blotting in the 2-day old control plants in the absence of
any inducing heat shock. At later stages of development and in the leaf
gradient only immunoreactivity with HSP 70 was observed. In contrast to the
levels of their mRNAs the highest levels of HSP 30-26 and 70 have been
observed in the basal segments indicating that translational control plays a
role during HSP expression. Under severe heat shock a protein of 30 kDa is
induced whose identity is not known but which reacts with the antibody to HSP
30-26 and might represent the accumulating precursors of the plastidic
proteins.
99 NAL Call. No.: 442.8 Z8
Expression of individual HMW glutenin subunit genes of wheat (Triticum
aestivum L.) in relation to differences in the number and type of homoeologous
subunits and differences in genetic background.
Kolster, P.; Krechting, C.F.; Gelder, W.M.J. van
Berlin, W. Ger. : Springer International; 1993 Oct.
Theoretical and applied genetics v. 87 (1/2): p. 209-216; 1993 Oct. Includes
references.
Language: English
Descriptors: Triticum aestivum; Complex loci; Structural genes; Glutenins;
Molecular weight; Gene expression; Lines; Alleles
Abstract: The amount of individual high-molecular-weight (HMW) glutenin
subunits of bread-wheat has been studied in relation to variation at
homoeologous loci and in the general genetic background. The relationships
between Glu-1 loci have been studied using near-isogenic lines (NILs) of the
variety Sicco and in the progenies of two crosses. Substitution of the Sicco
Glu-D1 allele by a null-allele resulted in higher amounts of the homoeologous
subunits. The presence of a Glu-A1 null-allele did not have a noticeable
effect on the amounts of homoeologous subunits. In three out of four NILs and
in the sister-lines of two crosses, the amounts of HMW-subunits did not depend
on the allele make-up at homoeologous loci. Only in the NIL which contains the
Glu-D1 allele, encoding subunits 1Dx2.2 and 1Dy12, was the amount of
homoeologous subunits lower than the amount of these subunits in Sicco. This
study suggests a relation between the amount of HMW-subunits encoded by an
allele and its contribution to bread-making quality. The effect of genetic
background has been studied using F4 and F5 lines of two crosses. The total
amounts of subunits, relative to the total amount of kernel proteins, showed a
considerable variation between lines. The ratio between individual subunits
did not differ between genetic backgrounds. Because this ratio is also largely
independent of differences in environmental conditions, it is concluded that
the relative amount of a subunit is a valuable measure for the detection of
genetically-determined differences in the expression of HMW-subunit genes.
100 NAL Call. No.: QK710.P68
Expression of maize Adh1 intron mutants in tobacco nuclei.
Lou, H.; McCullough, A.J.; Schuler, M.A.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993
Mar.
Language: English
Descriptors: Nicotiana; Zea mays; Gene transfer; Mutants; Transgenics; Nuclei;
Gene expression; Nucleotide sequences
101 NAL Call. No.: 382 P56
Expression of oat phyA cDNA in the moss Ceratodon purpureus.
Thummler, F.; Schuster, H.; Bonenberger, J.
Augusta, GA : American Society for Photobiology; 1992 Nov.
Photochemistry and photobiology v. 56 (5): p. 771-776; 1992 Nov. Includes
references.
Language: English
Descriptors: Mosses; Bryophyta; Genetic transformation; Avena sativa;
Protoplast fusion; Gene expression
Abstract: The possibility of transforming Ceratodon purpureus protoplasts by
PEG-mediated direct DNA uptake was tested. Transformation with a plasmid
carrying a kanamycin-resistance gene resulted in kanamycin-resistant colonies
of C. purpureus protonemata. A full-length cDNA clone coding for oat phyA
phytochrome was isolated. The clone HM4.1 which is, 3.7-kb long exhibits about
99% nucleotide sequence identity to the known phytochrome clone AP3. The
expression of HM4.1 in C. purpureus protonemata was tested. A construct with
the 35S-promotor and the structural gene of HM4.1 was cotransformed with the
plasmid containing the kanamycin-resistance. Kanamycin-resistant colonies were
tested for the presence of HM4.1 sequences in a genomic Southern experiment.
Two out of 19 kanamycin-resistant colonies reacted positively with a HM4.1
specific probe. The expression of phyA in the positive colonies was examined
with monoclonal antibodies specific for oat phytochrome. The Western blot
experiment with protein extracts of the two positive colonies grown in the
dark revealed clear signals at 124-kDa which were not detected in control
plants. These data demonstrate the possibility of expressing oat
phyA-apoprotein in C. purpureus protonemata. The transgenic moss protonemata
did not show phenotypical alterations in response to the foreign phytochrome
polypeptide; it is not known at the moment if the tetrapyrole chromophore is
attached to the oat polypeptide in the protonemata or not.
102 NAL Call. No.: 450 J8224
Expression of oat-phyA-cDNA in a suspension cell culture of transgenic
tobacco: a single-cell system for the study of phytochrome function.
McCormac, A.C.; Smith, H.; Whitelam, G.C.
Oxford : Oxford University Press; 1993 Jul.
Journal of experimental botany v. 264 (44): p. 1095-1103; 1993 Jul. Includes
references.
Language: English
Descriptors: Nicotiana tabacum; Avena sativa; Complementary DNA; Phytochrome;
Transgenic plants; Genetic transformation; Callus; Cell culture; Cell
suspensions; Gene expression; Red light; Far red light; Molecular
conformation; Genetic regulation; Proteolysis
Abstract: A culture of callus cells has been developed from a transgenic line
of tobacco which contains an introduced phyA-cDNA encoding phytochrome A.
Suspension cultures of the cells were shown to accumulate a significant
immunodetectable level of the heterologous phytochrome, but not of the native
phyA-gene product. The red-irradiated form (P(fr)) of the heterologous
phytochrome was specifically degraded in vivo, and the red-irradiated (P(fr))
and far-red-irradiated (P(r)) forms demonstrated different patterns of in
vitro proteolytic cleavage. These results strongly suggested that the
phytochrome apoprotein was associated with a chromophore moiety which mediated
red/far-red sensitive conformational changes of the molecule. Exogenous
application of 4-amino-5-hexynoic acid (AHA) to the transgenic suspension
cultures resulted in the accumulation of a population of phytochrome which was
stable under red light and gave identical patterns of in vitro digestion in
the red and far-red irradiated forms, i.e. the spectral activity of
phytochrome was inhibited. Application of exogenous 5-aminolevulinic acid
(ALA) or biliverdin overcame the inhibitory effects of AHA to restore spectral
sensitivity of the phytochrome pool. These results are consistent with the
proposed pathway of phytochrome chromophore biosynthesis in intact plant
systems. Thus, the transgenic suspension cultures provided a single-cell
system in which spectrally-active phytochrome, apparently indistinguishable
from the native phytochrome synthesized in etiolated seedlings, was
accumulated. Photoregulation of expression of the genes encoding the small
subunit of ribulose-1,5-bisphosphate carboxylase and chlorophyll a/b binding
proteins demonstrated that the heterosystem for the study of phytochrome
population mediated rapid changes in gene expression in the de-differentiated
cells. It is therefore proposed that such a suspension culture of transgenic
cells offers a model system for the study of phytochrome function.
103 NAL Call. No.: 450 P699
Expression of storage protein multigene families in developing rice endosperm.
Kim, W.T.; Li, X.X.; Okita, T.W.
Language: English
Descriptors: Oryza sativa; Multigene families; Structural genes; Glutelins;
Prolamins; Gene expression; Transcription; Messenger RNA; Endosperm; Seed
development
Abstract: Rice seeds accumulate both glutelins and prolamines as storage
proteins with the former polypeptides being the predominant reserve. To
evaluate the expression of the genes that encode for these proteins during
seed development, the transcription activities and mRNA levels of several gene
classes that comprise these multigene families were assessed. Results from
nuclear run-on transcription assays and RNA blot studies showed that the
expression of these gene classes for each multigene family was not coordinate
but instead differentially regulated at both the transcriptional and
post-transcriptional levels. Quantification of their total mRNA levels
revealed equimolar amounts of their mRNAs in 5 and 10 day old seeds and a 40%
excess of prolamine transcripts, relative to glutelin transcripts, in seeds of
15 days and older. In spite of the significant steady state levels of
prolamine transcripts, glutelin mRNAs were detected at two-fold greater excess
in membrane bound polysomes throughout seed development, thereby accounting
for, at least in part, the greater accumulation of this storage protein in
rice endosperm. These results suggest that, in addition to regulation at the
transcriptional/post-transcriptional levels, ER membrane-associated
translational control is also involved in the expression of rice seed storage
protein multigene families.
104 NAL Call. No.: 450 P692
Expression of the Acc1 gene-encoded acetyl-coenzyme A carboxylase in
developing maize (Zea mays L.) kernels.
Somers, D.A.; Keith, R.A.; Egli, M.A.; Marshall, L.C.; Gengenbach, B.G.;
Gronwald, J.W.; Wyse, D.L.
Language: English
Descriptors: Zea mays; Structural genes; Acetyl-coa carboxylase; Gene
expression; Seed development; Kernels; Enzyme activity; Endosperm; Plant
embryos; Sethoxydim
Abstract: A mutation (Acc1-S2) in the structural gene for maize (Zea mays L.)
acetyl-coenzyme A carboxylase (ACCase) that significantly reduces sethoxydim
inhibition of leaf ACCase activity was used to investigate the gene-enzyme
relationship regulating ACCase activity during oil deposition in developing
kernels. Mutant embryo and endosperm ACCase activities were more than 600-fold
less sensitive to sethoxydim inhibition than ACCase in wild-type kernel
tissues. Moreover, in vitro cultured mutant kernels developed normally in the
presence of sethoxydim concentrations that inhibited wild-type kernel
development. The results indicate that the Acc1-encoded ACCase accounts for
the majority of ACCase activity in developing maize kernels, suggesting that
Acc1-encoded ACCase functions not only during membrane biogenesis in leaves
but is also the predominant form of ACCase involved in storage lipid
biosynthesis in maize embryos.
105 NAL Call. No.: QK710.P68
Expression of the alpha-thionin gene from barley in tobacco confers enhanced
resistance to bacterial pathogens.
Language: English
Descriptors: Nicotiana tabacum; Hordeum vulgare; Agrobacterium tumefaciens;
Gene transfer; Transgenics; Gene expression; Thioneins; Protein synthesis;
Pathogenesis-related proteins; Disease resistance; Pseudomonas syringae pv.
tabaci
106 NAL Call. No.: 442.8 Z34
Expression of the gene encoding the PR-like protein PRms in germinating maize
embryos.
Language: English
Descriptors: Zea mays; Structural genes; Pathogenesis-related proteins; Gene
expression; Plant embryos; Seed germination; Genetic regulation; Defense
mechanisms; Scutellum; Gibberella fujikuroi; Fungal diseases; Cell wall
components; Gibberellic acid
Abstract: The PRms protein is a pathogenesis-related (PR)-like protein whose
mRNA accumulates during germination of maize seeds. Expression of the PRms
gene is induced after infection of maize seeds with the fungus Fusarium
moniliforme. To further our investigations on the expression of the PRms gene
we examined the accumulation of PRms mRNA in different tissues of maize
seedlings infected with F. moniliforme and studied the effect of fungal
elicitors, the mycotoxin moniliformin, the hormone gibberellic acid, and
specific chemical agents. Our results indicate that fungal infection, and
treatment either with fungal elicitors or with moniliformin, a mycotoxin
produced by F. moniliforme, increase the steady-state level of PRms mRNA. PRms
mRNA accumulation is also stimulated by the application of the hormone
gibberellic acid or by treatment with silver nitrate, whereas acetylsalicylic
acid has no effect. In situ RNA hybridization in isolated germinating embryo
sections demonstrates that the PRms gene is expressed in the scutellum,
particularly in a group of inner cells, and in the epithelium lying at the
interface of the scutellum and the endosperm. The pattern of expression of the
PRms gene closely resembles that found for hydrolytic enzymes, being confined
to the scutellum and the aleurone layer of the germinating maize seed. Our
results suggest that the PRms protein has a function during the normal process
of seed germination that has become adapted to serve among the defence
mechanisms induced in response to pathogens during maize seed germination.
107 NAL Call. No.: QK725.P532
Expression of the two maize TATA binding protein genes and function of the
encoded TBP proteins by complementation in yeast.
Vogel, J.M.; Roth, B.; Cigan, M.; Freeling, M.
Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Nov.
The Plant cell v. 5 (11): p. 1627-1638; 1993 Nov. Includes references.
Language: English
Descriptors: Zea mays; Saccharomyces cerevisiae; Structural genes; Multiple
genes; Dna binding proteins; Gene expression; Messenger RNA; Genetic
transformation; Complementation; Mutations; Mutants; Molecular mapping;
Linkage; Nucleotide sequences; Amino acid sequences; Complementary DNA
Abstract: A single gene encodes the TATA binding protein (TBP) in yeasts and
animals. Although two TBP-encoding genes (Tbp) previously were isolated from
both Arabidopsis and maize, the expression and in vivo function of the encoded
plant TBPs were not investigated. Here, we report that the two highly
conserved maize Tbp genes are unlinked and reside within larger, ancestrally
duplicated segments in the genome. We find quantitative differences in Tbp1
versus Tbp2 transcript accumulation in some maize tissues. These nonidentical
expression patterns may indicate differences in the tissue-specific regulation
of these genes, which might allow the two encoded maize TBP isoforms to
perform nonoverlapping functions in the plant. In addition, we show that the
maize TBP products, unlike animal TBPs, are functionally interchangeable with
yeast TBP for conferring yeast cell viability. This is a conclusive
demonstration of in vivo activity for a nonyeast TBP protein, and these
complementation results point to particular amino acids in TBP that are likely
to influence species-specific protein interactions.
108 NAL Call. No.: QK710.P62
Expression, organisation and structure of the genes encoding the waxy protein
(granule-bound starch synthase) in wheat.
Ainsworth, C.; Clark, J.; Balsdon, J.
Language: English
Descriptors: Triticum aestivum; Complementary DNA; Structural genes;
Hexosyltransferases; Loci; Gene expression; Messenger RNA; Filling period;
Seeds; Starch granules; Amino acid sequences
Abstract: A full-length cDNA clone representing the waxy protein (GBSSI)
isolated from a hexaploid wheat developing grain cDNA library has been used to
characterise the organization and expression of the waxy genes in wheat. The
genes are organised as a triplicate set of single copy homeoloci on chromosome
arms 4AL, 7AS and 7DS. The genes are active throughout grain filling where the
main 2.3 kb transcript accumulates to high levels. The 2.3 kb transcript is
not expressed in leaves where the presence of a related, but less homologous,
transcript of 1.6 kb suggests that a different set of genes operates. Gel
analysis and purification of the waxy protein isolated from starch granules,
followed by N-terminal amino acid sequencing in conjunction with data from
hybrid select translation experiments and sequence analysis of the cDNA, shows
that the mature protein has a molecular weight of 6OkDa (615 amino acids) and
that the preprotein includes a chloroplast/amyloplast transit peptide of 7kDa
(75 amino acids). Analysis of the derived amino acid sequence and alignment
with five other plant waxy proteins shows that they exhibit substantial
homology. The wheat protein differs from all others in that it contains an 11
amino acid insertion towards the N-terminus.The protein contains the conserved
motif KTGGL found in other waxy proteins and which has been implicated as the
active site in glycogen synthase.
109 NAL Call. No.: 442.8 Z8
Factors affecting transient gene expression in protoplasts isolated from very
slowly growing embryogenic callus cultures of wheat (Triticum aestivum L.).
Zaghmout, O.M.F.; Trolinder, N.L.
Language: English
Descriptors: Triticum aestivum; Vitis vinifera; Gene expression; Reporter
genes; Beta-glucuronidase; Recombinant DNA; Cauliflower mosaic caulimovirus;
Alcohol dehydrogenase; Promoters; Protoplasts; Electroporation; Genetic
transformation; Transgenic plants; Callus; Embryogenesis; Enzyme activity;
Histoenzymology; Tobacco mosaic tobamovirus; Nucleotide sequences; Plasmid
vectors; Regenerative ability
Abstract: Protoplasts isolated from embryogenic ('Mustang' and 'Chinese
Spring') and non-embryogenic ('Mit') calli of wheat (Triticum aestivum L.)
genotypes transiently expressed beta-glucuronidase (GUS) activity when
electroporated with a plasmid containing the GUS gene and driven by an
enhanced 35S promoter and a TMV leader sequence. Conditions for the maximum
expression of GUS activity were: electroporation of the freshly isolated
protoplasts at 250 Vcm- and 250 microF for 2 s using 50 microgram/ml of
plasmid DNA; incubation of the protoplasts with the plasmid before the pulse
for 2 h; and a 15-min recovery period on ice after the pulse. In general, a
higher GUS activity was obtained in protoplasts of non-embryogenic (NE) callus
origin than in those of embryogenic (E) callus origin. Only GUS constructs
containing a duplicate 35S promoter derivative resulted in a significant level
of GUS expression. The presence of the TMV viral leader sequence in the
pAGUS1-TN2 plasmid construct resulted in a significant increase of GUS
activity in the electroporated protoplasts of both callus types. On the other
hand, protoplasts electroporated with the Adh1 promoter and intron showed a
threefold less GUS activity than those electroporated with pAGUS1-TN2.
Optimized conditions for DNA uptake and expression were very similar for
protoplasts of both callus types. The importance of these findings for the
successful regeneration of transgenic and fertile wheat plants is discussed.
110 NAL Call. No.: QK710.P62
Factors influencing Agrobacterium-mediated transient expression of gusA in
rice.
Language: English
Descriptors: Oryza sativa; Agrobacterium tumefaciens; Genetic transformation;
Gene expression; Reporter genes; Beta-glucuronidase; Gene transfer; Plasmids;
Transgenics; Genetic regulation; 2,4-d; Culture; Explants; Leaves; Roots;
Seeds; Shoots; Amino acid derivatives
Abstract: Transient expression of GUS in rice (Oryza sativa L.) mediated by
Agrobacterium tumefaciens was characterized using binary vectors containing
gusA genes that express minimal (pKIWI105 and pCNL1) or no (p35S-GUS-INT and
pCNL56) GUS activity in bacteria. Four-day old seedlings obtained from seeds
or immature embryos of rice were cut into shoot, root, and seed remnants and
inoculated with various strains of A. tumefaciens. Transient GUS expression
events were quantitated histochemically by determining the frequency of
explants exhibiting blue spots indicative of GUS at four to six days after
cocultivation with A. tumefaciens. A. tumefaciens strains that did not contain
the gusA gene (At643) or a Ti-plasmid (At563 and At657) did not elicit any
blue staining characteristic of GUS activity. Several parameters were
important in obtaining efficient transient expression of GUS in rice mediated
by A. tumefaciens. The growth regulator 2,4-D inhibited GUS expression if
present during the seed germination period, but the presence of 6 mg/l 2,4-D
during cocultivation of the explants with A. tumefaciens slightly enhanced GUS
expression efficiency. All 21 rice cultivars tested expressed GUS after
co-cultivation with A. tumefaciens. The GUS expression frequency was highest
amongst the indica cultivars. The frequencies of GUS expression in japonica
cultivars and in Oryza glaberrima cultivars (grown primarily in Africa) were
generally one-half to one-third the level found for indica varieties. Leaf
explants were more susceptible to A. tumefaciens-facilitated GUS expression
than were roots or seed remnants. The vir genes of an agropine-type Ti-plasmid
of A. tumefaciens were most effective in directing transient GUS expression in
rice, whereas those of a nopaline-type and an octopine-type plasmid were less
effective. We have also found that the frequency of transient expression of
GUS was higher with pBIN19 as the precursor cloning vector than with pEND4K as
the precursor cloning vector. Reasons for differences in effectiveness of
these binary vectors are discussed. Using the conditions described here, A.
tumefaciens-mediated frequencies of transient GUS expression in four-day old
shoot of several rice cultivars were routinely in excess of 50%.
111 NAL Call. No.: 450 P692
Five genes induced by aluminum in wheat (Triticum aestivum L.) roots.
Snowden, K.C.; Gardner, R.C.
Language: English
Descriptors: Triticum aestivum; Root tips; Aluminum; Treatment; Dna; Gene
expression; Nucleotide sequences; Clones; Tolerance; Phytotoxicity
Abstract: Five different cDNAs (termed wali1 to wali5 for wheat aluminum
induced) whose expression was induced by Al stress have been isolated from the
root tips of Al-treated wheat (Triticum aestivum L.) plants. Four of these
genes were induced 24 to 96 h after Al treatment, and their expression is
reduced when the Al is removed. Each of these four genes was induced by
inhibitory levels of Al in two wheat cultivar's--Warigal, an Al-sensitive
cultivar, and Waalt, an Al-tolerant cultivar. The fifth gene (wali2) showed a
complex bimodal pattern of induction and was induced by Al only in the
sensitive cultivar. Comparison of the nucleotide sequences of these clones to
those in the sequence data bases showed that wali4 is homologous to
phenylalanine ammonia-lyase and wali1 is homologous to a group of plant
proteins that are cysteine-rich and have homology to metallothioneins. wali2
encodes a novel protein with a repeating motif of cysteine amino acids. The
remaining two wali clones (wali3 and wali5) encode related, cysteine-rich
proteins that show no significant homology to any known sequences.
112 NAL Call. No.: QP601.M49
Foreign gene expression in chloroplasts of higher plants mediated by Tungsten
particle bombardment.
Language: English
Descriptors: Triticum aestivum; Nicotiana tabacum; Beta vulgaris;
Chloroplasts; Genetic transformation; Recombinant DNA; Gene expression
113 NAL Call. No.: QK710.P68
Four members of the maize beta-tubulin gene family are expressed in the male
gametophyte.
Language: English
Descriptors: Zea mays; Amino acid sequences; Clones; Dna; Tubulin; Gametes;
Gene expression; Males; Nucleotide sequences
114 NAL Call. No.: QH442.A1G4
The gene encoding a calcium-dependent protein kinase located near the sbe1
gene encoding starch branching enzyme I is specifically expressed in
developing rice seeds.
Language: English
Descriptors: Oryza sativa; Structural genes; Complementary DNA; Protein
kinase; Calcium ions; Binding site; Nucleotide sequences; Amino acid
sequences; Gene mapping; Gene expression; Seed development; Calmodulin
Abstract: A gene (spk) encoding a Ca(2+)-dependent protein kinase (SPK) is
located in the region immediately upstream of the sbe1 gene encoding a starch
branching enzyme. The spk gene is specifically expressed in developing seeds
and its expression pattern is very similar to those of genes encoding
starch-synthesizing enzymes such as sbel and waxy, seed lipid-synthesizing
enzymes, as well as genes encoding seed storage proteins. A full-length spk
cDNA was isolated from a cDNA library constructed from developing seeds. The
deduced amino acid sequence showed that SPK has a high degree of homology to
soybean and carrot Ca(2+)-dependent protein kinase, both of which contain
calmodulin domains. The calmodulin domain, as well as the catalytic subdomain
consensus regions of protein kinases are highly conserved in SPK. These
results suggest that a tissue- and stage-specific protein kinase, SPK, is
involved in the synthesis of seed storage compounds during seed development.
They also strongly suggest that Ca(2+) is required for seed development.
115 NAL Call. No.: QK710.P62
Gene structure and expression of rice seed allergenic proteins belonging to
the alpha-amylase/trypsin inhibitor family.
Adachi, T.; Izumi, H.; Yamada, T.; Tanaka, K.; Takeuchi, S.; Nakamura, R.;
Matsuda, T.
Language: English
Descriptors: Oryza sativa; Structural genes; Dna; Seeds; Enzyme inhibitors;
Alpha-amylase; Trypsin inhibitors; Nucleotide sequences; Promoters; Amino acid
sequences; Prediction; Multigene families; Gene expression; Seed development;
Messenger RNA; Allergens; Complementary DNA
Abstract: Genomic and two novel cDNA clones for rice seed allergenic protein
(RA) belonging to the alpha-amylase/trypsin inhibitor family were isolated and
their nucleotide sequences determined. Ten cysteine residues deduced from
nucleotide sequences were completely conserved among three cDNA clones
including a clone, RA17, reported previously. One genomic clone, lambda 4,
contained two RA genes, RAG1 and RAG2. Although RAG1 was cloned at the 5'
portion only, two RA genes were arranged divergently. Nucleotide sequencing
and DNA blotting analyses showed that RA are encoded by a multigene family
consisting of at least four members. The transcriptional initiation site of
RAG1 was localized at A, 26 bp upstream of the putative translational
initiation codon, ATG, by the primer extension assay. The putative TATA box
and CAAT box existed about 45 bp and 147 bp upstream of the transcription
initiation site, respectively. A conserved sequence (ATGCAAAA) which was
similar to the sequence (TGCAAAA) identified in rice glutelin promoters was
observed in the 5' region of the two genes. In addition, RNA blotting analyses
provided that RA genes specifically expressed in ripening seed and their
transcripts accumulated maximally between 15 and 20 days after flowering.
116 NAL Call. No.: QK728.P52 1992
Gene transfer to barley.
Language: English
Descriptors: Hordeum vulgare; Gene transfer; Direct DNAuptake;
Inflorescences; Genetic transformation; Protoplasts; Pollen tubes; Gene
expression
117 NAL Call. No.: QK725.P54
Gene transfer to maize male reproductive structure by particle bombardment of
tassel primordia.
Language: English
Descriptors: Zea mays; Pollen; Gene transfer; Dna; Tassels; Anther culture;
Gene expression; Beta-glucuronidase; Anthocyanins; Marker genes; Culture
techniques
Abstract: Maize (Zea mays L.) tassel primordia were used as a target for
particle bombardment, to assess the possibility of introducing foreign DNA
into male reproductive structures. Transient expression of the
beta-glucuronidase gene (GUS) or anthocyanin marker genes (C1 and B-Peru)
driven by the CaMV 35S promoter was obtained in tassel primordia 24h after
bombardment. Gold particles coated with DNA reached stamen primordia tissues,
which eventually form the anthers and pollen. Bombarded tassels were also
cultured in vitro and GUS activity was detected in the vascular tissue of
mature anthers that developed within 4 weeks. This new approach represents a
preliminary step toward pollen mediated transformation.
118 NAL Call. No.: QH301.A76
Genetic control of frost tolerance.
Language: English
Descriptors: Hordeum vulgare; Cloning; Frost resistance; Gene expression;
Genetic regulation; Inheritance; Temperature; Acclimatization; Biochemistry
119 NAL Call. No.: 59.8 C333
Genetic engineering and hybridization of wheat.
Kureczka, J.E.
Language: English
Descriptors: Wheat; Hybridization; Genetic engineering; Genetic
transformation; Gene expression; Food quality
Abstract: Experts say the creation of useful-new varieties of wheat through
genetic engineering requires success in three discrete areas. First, genetic
transformation technologies must be perfected for use in wheat. Second,
commercially useful genes and expression systems must be isolated and made
available. Finally, and perhaps most importantly from a business standpoint,
new hybridization technologies must be developed that work efficiently with
this normally self-pollinating grain.
120 NAL Call. No.: QK725.P532
Genetic isolation, cloning, and analysis of a Mutator-induced, dominant
antimorph of the maize amylose extender1 locus.
Stinard, P.S.; Robertson, D.S.; Schnable, P.S.
Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Nov.
The Plant cell v. 5 (11): p. 1555-1566; 1993 Nov. Includes references.
Language: English
Descriptors: Antirrhinum majus; Loci; Induced mutations; Structural genes;
Kinases; Dominance; Genetic polymorphism; Repetitive DNA; Transposable
elements; Gene expression; Transcription; Messenger RNA; Endosperm;
Restriction mapping
Abstract: We report the genetic identification, molecular cloning, and
characterization of a dominant mutant at the amylose extender1 locus,
Ae1-5180. The identities of our clones are corraborated by their ability to
reveal DNA polymorphisms between seven wild-type revertants from Ae1-5180
relative to the Ae1-5180 mutant allele and between four of five independently
derived, Mutator (Mu)-induced recessive ae1 alleles relative to their
respective wild-type progenitor alleles. The Ae1-5180 mutation is associated
with two Mu1 insertions flanked by complex rearrangements of ae1-related
sequences. One of the Mu1 elements is flanked by inverted repeats of
ae1-related DNA of at least 5.0 kb in length. This Mu1 element and at least
some of this flanking inverted repeat DNA are absent or hypermethylated in six
of seven wild-type revertants of Ae1-5180 that were analyzed. The second Mu1
element is flanked on one side by the 5.0-kb ae1-specific repeat and on the
other side by a sequence that does not hybridize to the ae1-related repeat
sequence. This second Mu1 element is present in revertants to the wild type
and does not, therefore, appear to affect ae1 gene function. A 2.7-kb ae1
transcript can be detected in wild-type and homozygous ae1-Ref endosperms 20
days after pollination. This transcript is absent in endosperms containing
one, two, or three doses of Ae1-5180. This result is consistent with a
suppression model to explain the dominant gene action of Ae1-5180 and
establishes Ae1-5180 as an antimorphic allele. Homozygous wild-type seedlings
produce no detectable transcript, indicating some degree of tissue specificity
for ae1 expression. Sequence analyses establish that ae1 encodes starch
branching enzyme II.
121 NAL Call. No.: S494.5.B563C87
Genetic variation in ABA production in maize determines the extent of
drought-induced gene transcription.
Language: English
Descriptors: Zea mays; Transcription; Gene expression; Water stress; Drought;
Abscisic acid; Biosynthesis; Genetic variation; Protein synthesis; Plant
proteins
122 NAL Call. No.: QK710.P68
A gibberelin-regulated gene from wheat with sequence homology to cathepsin B
of mammalian cells.
Language: English
Descriptors: Triticum; Amino acid sequences; Cathepsins; Dna; Gene expression;
Genetic code; Genetic regulation; Gibberellins; Messenger RNA; Nucleotide
sequences; Transcription
123 NAL Call. No.: S494.5.B563C87
The gibberellin response element: a DNA sequence in cereal alpha-amylase gene
promoters that mediates GA and ABA effects.
Rogers, J.C.; Lanahan, M.B.; Rogers, S.W.; Mundy, J.
Dordrecht : Kluwer Academic Publishers; 1992.
Current plant science and biotechnology in agriculture v. 13: p. 136-146;
1992. In the series analytic: Progress in plant growth regulation / edited by
C.M. Karssen, L.C. Van Loon and D. Vreugdenhil. Proceedings of the 14th
International Conference on Plant Growth Substances held July 21-26, 1991,
Amsterdam, Netherlands. Includes references.
Language: English
Descriptors: Hordeum vulgare; Triticum aestivum; Avena sativa; Promoters;
Binding site; Dna binding proteins; Alpha-amylase; Structural genes; Gene
expression; Transcription; Messenger RNA; Genetic regulation; Gibberellic
acid; Abscisic acid; Aleurone layer; Literature reviews
124 NAL Call. No.: QK725.P532
Gibberellin-responsive elements in the promoter of a barley high-pl
alpha-amylase gene.
Language: English
Descriptors: Hordeum vulgare; Promoters; Alpha-amylase; Controlling elements;
Gibberellic acid; Abscisic acid; Genetic regulation; Gene expression;
Beta-glucuronidase; Reporter genes; Targeted mutagenesis; Recombinant DNA;
Transcription
Abstract: Deletion analysis has previously shown that the major gibberellic
acid (GA)- and abscisic acid (ABA)-responsive elements in the promoter of a
high-pI alpha-amylase gene of barley are located downstream of -174 (Jacobsen
and Close, 1991). We have used transient expression assays in barley aleurone
protoplasts to identity sequences between -174 and +53 that confer GA and ABA
responsiveness on expression of a beta-glucuronidase reporter gene. Using
alpha-amylase promoter fragments and synthetic oligonucleotides fused to
minimal promoters, we have shown that the hormone-responsive region is located
between -174 and -108. A single copy of this region fused to a minimal
alpha-amylase promoter (-41) conferred both GA- and ABA-responsive expression
on the reporter gene comparable to the positive control, Am(-174)IGN. Multiple
copies of this region were able to activate even greater levels of expression.
Site-directed mutagenesis was used to determine the functional importance of
the conserved motifs ((-169)pyrimidine box, (-143)TAACAAA box, and
(-124)TATCCAC box) and nonconserved intervening sequences within the region
between -174 and -108. Our results showed that both the TAACAAA and TATCCAC
boxes play an important role in GA-regulated expression. We propose that the
TAACAAA box is a gibberellin response element, that the TATCCAC box acts
cooperatively with the TAACAAA box to give a high level of GA-regulated
expression, and that together these motifs form important components of a
gibberellin response complex in high-pI alpha-amylase genes. The TAACAAA box
also appears to be the site of action of ABA. In addition, we have identified
a sequence that acts as a repressor of GA action and that resembles a cAMP
response element.
125 NAL Call. No.: 450 P692
Glutamine induces the N-dependent accumulation of mRNAs encoding
phosphoenolpyruvate carboxylase and carbonic anhydrase in detached maize leaf
tissue.
Language: English
Descriptors: Zea mays; Structural genes; Messenger RNA; Phosphoenolpyruvate
carboxylase; Carbonate dehydratase; Gene expression; Genetic regulation;
Glutamine; Leaves; Nitrate; Glutamic acid; Alanine; Serine; Glycine; Enzyme
activity; Glutamate-ammonia ligase
Abstract: We have used detached leaves to study the N-dependent control of
expression of phosphoenolpyruvate carboxylase (PEPC) and carbonic anhydrase
(CA) genes in maize (Zea mays L. cv Golden Cross Bantam T51). Following
supplementation with an N-source and zeatin, PEPC and CA mRNA levels increased
in leaves detached from N-deficient maize plants. Addition of methionine
sulfoximine (MSX), a specific inhibitor of glutamine synthetase, inhibited the
nitrate-dependent increase of PEPC and CA mRNA but did not affect the
glutamine-dependent increase of PEPC and CA mRNA levels. Glutamine levels in
detached maize leaves treated with various N sources in the presence or
absence of MSX correlated with the levels of PEPC and CA mRNA. We conclude
that glutamine is the most likely effector for controlling the N-dependent
expression of PEPC and CA in maize plants.
Aukerman, M.J.; Schmidt, R.J.
Dordrecht : Kluwer Academic Publishers; 1993 Jan.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (2): p. 355-362; 1993 Jan.
Includes references.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers in
association with the Society for Experimental Biology, c1991-; 1993 Sep.
The Plant journal : for cell and molecular biology v. 4 (3): p. 535-544; 1993
Sep. Includes references.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers in
association with the Society for Experimental Biology, c1991-; 1993 Aug.
The Plant journal : for cell and molecular biology v. 4 (2): p. 357-366; 1993
Aug. Includes references.
PUSDAx
NSUQK1.P73
Han, C.D.; Patrie, W.; Polacco, M.; Coe, E.H. Jr
Berlin ; New York : Springer-Verlag, 1925-; 1993.
Planta v. 191 (4): p. 552-563; 1993. Includes references.
Oxford, Eng. : IRL Press; 1993 Feb.
The EMBO journal - European Molecular Biology Organization v. 12 (2): p.
651-657; 1993 Feb. Includes references.
Oxford, Eng. : IRL Press; 1993 Feb.
The EMBO journal - European Molecular Biology Organization v. 12 (2): p.
651-657; 1993 Feb. Includes references.
Hughes, M.A.; Dunn, M.A.; Pearce, R.S.; White, A.J.; Zhang, L.
Oxford : Blackwell Scientific Publications; 1992 Sep.
Plant, cell and environment v. 15 (7): p. 861-865; 1992 Sep. Includes
references.
Balconi, C.; Rizzi, E.; Motto, M.; Salamini, F.; Thompson, R.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993
Feb.
The plant journal v. 3 (2): p. 325-334; 1993 Feb. Paper presented at the
"Symposium on the use of Mutants to Study Plant Metabolism and Development,"
Annual Meeting of the Society of Experimental Biology, April, 1992. Includes
references.
Nucleic acids research v. 21 (4): p. 969-975; 1993 Feb25. Includes
references.
Rockville, Md. : American Society of Plant Physiologists; 1993 Jan.
Plant physiology v. 101 (1): p. 227-284; 1993 Jan. Includes references.
Weinheim ; New York : VCH; 1993.
Plant mitochondria : with emphasis on RNA editing and cytoplasmic male
sterility /. p. 207-219; 1993. Includes references.
Varagona, M.J.; Purugganan, M.; Wessler, S.R.
Rockville, Md. : American Society of Plant Physiologists; 1992 Jul.
The Plant cell v. 4 (7): p. 811-820; 1992 Jul. Includes references.
Rigau, J.; Capellades, M.; Montoliu, L.; Torres, M.A.; Romera, C.;
Martinez-Izquierdo, J.A.; Tagu, D.; Puigdomenech, P.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers in
association with the Society for Experimental Biology, c1991-; 1993 Dec.
The Plant journal : for cell and molecular biology v. 4 (6): p. 1043-1050;
1993 Dec. Includes references.
Vellanoweth, R.L.; Okita, T.W.
Dordrecht : Kluwer Academic Publishers; 1993 Apr.
Plant molecular biology v. 22 (1): p. 25-41; 1993 Apr. Includes references.
Cejudo, F.J.; Ghose, T.K.; Stabel, P.; Baulcombe, D.C.
Dordrecht : Kluwer Academic Publishers; 1992 Dec.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 20 (5): p. 849-859; 1992 Dec.
Includes references.
The plant journal v. 3 (4): p. 509-518; 1993 Apr. Includes references.
Dordrecht : Kluwer Academic Publishers; 1993 Aug.
Plant molecular biology v. 22 (5): p. 829-846; 1993 Aug. Includes references.
Brandt, J.; Nielsen, V.S.; Thordal-Christensen, H.; Simpson, D.J.; Okkels,
J.S.
Dordrecht : Kluwer Academic Publishers; 1992 Jul.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 19 (4): p. 699-703; 1992 Jul.
Includes references.
Heck, G.R.; Chamberlain, A.K.; Ho, T.H.D.
Berlin, W. Ger. : Springer International; 1993 May.
Molecular & general genetics : MGG v. 239 (1/2): p. 209-218; 1993 May.
Includes references.
Berlin, W. Ger. : Springer International; 1993.
Plant cell reports v. 12 (7/8): p. 445-452; 1993. Includes references.
Nash, J.; Walbot, V.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Sep.
Plant physiology v. 100 (1): p. 464-471; 1992 Sep. Includes references.
Physiological and molecular plant pathology v. 40 (6): p. 395-409; 1992 Jun.
Includes references.
Dordrecht : Kluwer Academic Publishers; 1992 Oct.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 20 (2): p. 323-326; 1992 Oct.
Includes references.
Reimmann, C.; Dudler, R.
Rockville, Md. : American Society of Plant Physiologists; 1993 Mar.
Plant physiology v. 101 (3): p. 1113-1114; 1993 Mar. Includes references.
Joanin, P.; Gigot, C.; Philipps, G.
Dordrecht : Kluwer Academic Publishers; 1993 Feb.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (4): p. 701-704; 1993 Feb.
Includes references.
Joanin, P.; Gigot, C.; Philipps, G.
Dordrecht : Kluwer Academic Publishers; 1993 Feb.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (4): p. 701-704; 1993 Feb.
Includes references.
Columbus, Ohio : Botanical Society of America; 1992 Jul.
American journal of botany v. 79 (7): p. 778-783; 1992 Jul. Includes
references.
Washington, D.C. : The Academy; 1993 May01.
Proceedings of the National Academy of Sciences of the United States of
America v. 90 (9): p. 4057-4061; 1993 May01. Includes references.
Fincher, G.B.
Wallingford, Oxford, UK : CAB International; 1992.
Biotechnology in agriculture (5): p. 413-437; 1992. In the series analytic:
Barley : genetics, biochemistry, molecular biology and biotechnology / edited
by P.R. Shewry. Includes references.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Oct.
Plant physiology v. 100 (2): p. 915-922; 1992 Oct. Includes references.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993
Apr.
The plant journal v. 3 (4): p. 527-536; 1993 Apr. Includes references.
New York, N.Y. : Wiley-Liss, Inc; 1993.
Developmental genetics v. 14 (1): p. 27-41; 1993. In the special issue: Focus
on heat shock genes (part 1) / edited by J.J. Heikkila. Includes references.
The EMBO journal - European Molecular Biology Organization v. 12 (2): p.
563-571; 1993 Feb. Includes references.
The EMBO journal - European Molecular Biology Organization v. 12 (2): p.
563-571; 1993 Feb. Includes references.
Beator, J.; Kloppstech, K.
New York, N.Y. : Plenum Press; 1992.
NATO ASI series : Series A : Life sciences v. 226: p. 101-106. ill; 1992. In
the series analytic: Regulation of chloroplast biogenesis / edited by J.H.
Argyroudi-Akoyunoglou. Proceedings of a NATO Advanced Research Workshop, July
28-August 3, 1991, Crete, Greece. Includes references.
Dordrecht : Kluwer Academic Publishers; 1993 Apr.
Plant molecular biology v. 22 (1): p. 165-170; 1993 Apr. Includes references.
Pla, M.; Vilardell, J.; Guiltinan, M.J.; Marcotte, W.R.; Niogret, M.F.;
Quatrano, R.S.; Pages, M.
Dordrecht : Kluwer Academic Publishers; 1993 Jan.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (2): p. 259-266; 1993 Jan.
Includes references.
Szell, M.; Szekeres, M.; Adam, E.; Fejes, E.; Nagy, F.
New York, N.Y. : Plenum Press; 1992.
NATO ASI series : Series A : Life sciences v. 226: p. 57-61; 1992. In the
series analytic: Regulation of chloroplast biogenesis / edited by J.H.
Argyroudi-Akoyunoglou. Proceedings of a NATO Advanced Research Workshop, July
28-August 3, 1991, Crete, Greece. Includes references.
Rockville, Md. : American Society of Plant Physiologists; 1992 Aug.
Plant physiology v. 99 (4): p. 1381-1387; 1992 Aug. Includes references.
Medina, J.; Hueros, G.; Carbonero, P.
Dordrecht : Kluwer Academic Publishers; 1993 Nov.
Plant molecular biology v. 23 (3): p. 532-542; 1993 Nov. Includes references.
Amsterdam : Elsevier Science Publishers; 1993.
Gene v. 130 (2): p. 159-166; 1993. Includes references.
Reimmann, C.; Ringli, C.; Dudler, R.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.
Plant physiology v. 100 (3): p. 1611-1612; 1992 Nov. Includes references.
Mujer, C.V.; Rumpho, M.E.; Lin, J.J.; Kennedy, R.A.
Rockville, Md. : American Society of Plant Physiologists; 1993 Jan.
Plant physiology v. 101 (1): p. 217-226; 1993 Jan. Includes references.
Wallingford, Oxford, UK : CAB International; 1992.
Biotechnology in agriculture (5): p. 319-333; 1992. In the series analytic:
Barley : genetics, biochemistry, molecular biology and biotechnology / edited
by P.R. Shewry. Includes references.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.
Plant physiology v. 100 (3): p. 1384-1388; 1992 Nov. Includes references.
New York, NY : Springer-Verlag New York Inc; 1992 Nov.
European journal of biochemistry v. 209 (3): p. 933-937; 1992 Nov. Includes
references.
Berlin, W. Ger. : Springer International; 1993 Jan.
M G G : Molecular and general genetics v. 236 (2/3): p. 155-162; 1993 Jan.
Includes references.
St. Paul, MN : APS Press, [c1987-; 1993 Nov.
Molecular plant-microbe interactions : MPMI v. 6 (6): p. 745-754; 1993 Nov.
Includes references.
Sugiharto, B.; Burnell, J.N.; Sugiyama, T.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Sep.
Plant physiology v. 100 (1): p. 153-156; 1992 Sep. Includes references.
Veen, R. van der; Heimovaara-Dijkstra, S.; Wang, M.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Oct.
Plant physiology v. 100 (2): p. 699-705; 1992 Oct. Includes references.
Rogers, J.C.; Rogers, S.W.
Rockville, Md. : American Society of Plant Physiologists; 1992 Nov.
The Plant cell v. 4 (11): p. 1443-1451; 1992 Nov. Includes references.
Molina, A.; Garcia-Olmedo, F.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers in
association with the Society for Experimental Biology, c1991-; 1993 Dec.
The Plant journal : for cell and molecular biology v. 4 (6): p. 983-991; 1993
Dec. Includes references.
Rockville, Md. : American Society of Plant Physiologists; 1992 Jul.
Plant physiology v. 99 (3): p. 1226-1231; 1992 Jul. Includes references.
Dordrecht : Kluwer Academic Publishers; 1992.
Current plant science and biotechnology in agriculture v. 13: p. 493-499;
1992. In the series analytic: Progress in plant growth regulation / edited by
C.M. Karssen, L.C. Van Loon and D. Vreugdenhil. Proceedings of the 14th
International Conference on Plant Growth Substances held July 21-26, 1991,
Amsterdam, Netherlands. Includes references.
Becker, W.; Apel, K.
Berlin ; New York : Springer-Verlag, 1925-; 1993.
Planta v. 189 (1): p. 74-79; 1993. Includes references.
Berlin, W. Ger. : Springer International; 1992 Sep.
Theoretical and applied genetics v. 84 (7/8): p. 941-946; 1992 Sep. Includes
references.
Dordrecht : Kluwer Academic Publishers; 1993 Oct.
Plant molecular biology v. 23 (2): p. 401-407; 1993 Oct. Includes references.
Acevedo, A.; Scandalios, J.G.
Kyoto : Japanese Society of Plant Physiologists; 1992 Dec.
Plant and cell physiology v. 33 (8): p. 1079-1088; 1992 Dec. Includes
references.
Leader, D.; Connelly, S.; Filipowicz, W.; Waugh, R.; Brown, J.W.S.
Dordrecht : Kluwer Academic Publishers; 1993 Jan.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (1): p. 133-143; 1993 Jan.
Includes references.
Mauch, F.; Dudler, R.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug.
Plant physiology v. 102 (4): p. 1193-1201; 1993 Aug. Includes references.
Butler, W.M.; Cumming, A.C.
Berlin ; New York : Springer-Verlag, 1925-; 1993.
Planta v. 189 (1): p. 47-54; 1993. Includes references.
Wien : Springer; 1993.
Plant systematics and evolution v. 185 (3/4): p. 181-188; 1993. Includes
references.
Jupe, E.R.; Zimmer, E.A.
Dordrecht : Kluwer Academic Publishers; 1993 Mar.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (5): p. 805-821; 1993 Mar.
Includes references.
Washington, D.C. : National Academy of Sciences,; 1993 Aug01.
Proceedings of the National Academy of Sciences of the United States of
America v. 90 (15): p. 7094-7098; 1993 Aug01. Includes references.
Kawaguchi, H.; Fukuda, I.; Shiina, T.; Toyoshima, Y.
Dordrecht : Kluwer Academic Publishers; 1992 Nov.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 20 (4): p. 695-704; 1992 Nov.
Includes references.
Berlin, W. Ger. : Springer International; 1993.
Plant cell reports v. 12 (9): p. 506-509; 1993. Includes references.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Dec.
Plant physiology v. 100 (4): p. 1780-1786; 1992 Dec. Includes references.
Meulen, R.M. van der; Heidekamp, F.; Jastorff, B.; Horgan, R.; Wang, M.
New York : Springer-Verlag New York, c1982-; 1993.
Journal of plant growth regulation v. 12 (1): p. 13-19; 1993. Includes
references.
Mendu, N.; Siflow, C.D.
Kyoto, Japan : Japanese Society of Plant Physiologists; 1993 Oct.
Plant and cell physiology v. 34 (7): p. 973-983; 1993 Oct. Includes
references.
Fan, Y.L.; Zhou, X.J.
Dordrecht : Kluwer Academic Publishers; 1993.
Current plant science and biotechnology in agriculture v. 15: p. 169-173;
1993. In the series analytic: Biotechnology in Agriculture / edited by C.
You, Z. Chen, Y. Ding. Proceedings of the First Asia-Pacific Conference on
Agricultural Biotechnology held August 20-24, 1992, Beijing, China. Includes
references.
Berlin, W. Ger. : Springer International; 1993.
Plant cell reports v. 12 (9): p. 491-495; 1993. Includes references.
Boyer, S.K.; Shotwell, M.A.; Larkins, B.A.
Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1992
Aug25.
The Journal of biological chemistry v. 267 (24): p. 17449-17457; 1992 Aug25.
Includes references.
Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.
Plant physiology v. 99 (2): p. 693-699; 1992 Jun. Includes references.
Masoud, S.A.; Johnson, L.B.; White, F.F.; Reeck, G.R.
Dordrecht : Kluwer Academic Publishers; 1993 Feb.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (4): p. 655-663; 1993 Feb.
Includes references.
Nakanishi, H.; Okumura, N.; Umehara, Y.; Nishizawa, N.; Chino, M.; Mori, S.
Kyoto : Japanese Society of Plant Physiologists; 1993 Apr.
Plant and cell physiology v. 34 (3): p. 401-410; 1993 Apr. Includes
references.
Toki, S.; Takamatsu, S.; Nojiri, C.; Ooba, S.; Anzai, H.; Iwata, M.;
Christensen, A.H.; Quail, P.H.; Uchimiya, H.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.
Plant physiology v. 100 (3): p. 1503-1507; 1992 Nov. Includes references.
Matsuoka, M.; Ichikawa, H.; Saito, A.; Tada, Y.; Fujimura, T.; Kano-Murakami,
Y.
Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Sep.
The Plant cell v. 5 (9): p. 1039-1048; 1993 Sep. Includes references.
Dordrecht : Kluwer Academic Publishers; 1993.
Current plant science and biotechnology in agriculture v. 15: p. 245-249;
1993. In the series analytic: Biotechnology in Agriculture / edited by C.
You, Z. Chen, Y. Ding. Proceedings of the First Asia-Pacific Conference on
Agricultural Biotechnology held August 20-24, 1992, Beijing, China. Includes
references.
Berlin, W. Ger. : Springer International; 1992 Dec.
Theoretical and applied genetics v. 85 (4): p. 407-414; 1992 Dec. Includes
references.
Meldgaard, M.
Berlin, W. Ger. : Springer International; 1992.
Theoretical and applied genetics v. 83 (6/7): p. 695-706; 1992. Includes
references.
Moneger, F.; Mandaron, P.; Niogret, M.F.; Freyssinet, G.; Mache, R.
Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.
Plant physiology v. 99 (2): p. 396-400; 1992 Jun. Includes references.
Dordrecht : Kluwer Academic Publishers; 1993 Oct.
Plant molecular biology v. 23 (1): p. 111-122; 1993 Oct. Includes references.
The plant journal v. 3 (3): p. 393-403; 1993 Mar. Includes references.
Kyoto, Japanese Society of Plant Physiologists; 1993 Jun.
Plant and cell physiology v. 34 (4): p. 595-603; 1993 Jun. Includes
references.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Mar.
Plant physiology v. 101 (3): p. 1097-1101; 1993 Mar. Includes references.
Carmona, M.J.; Molina, A.; Fernandez, J.A.; Lopez-Fando, J.J.; Garcia-Olmedo,
F.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993
Mar.
The plant journal v. 3 (3): p. 457-462; 1993 Mar. Includes references.
Casacuberta, J.M.; Raventos, D.; Puigdomenech, P.; San Segundo, B.
Berlin, W. Ger. : Springer International; 1992 Jul.
M G G : Molecular and general genetics v. 234 (1): p. 97-104; 1992 Jul.
Includes references.
Dordrecht : Kluwer Academic Publishers; 1993 Apr.
Plant molecular biology v. 22 (1): p. 67-82; 1993 Apr. Includes references.
Berlin, W. Ger. : Springer International; 1993 Jul.
Theoretical and applied genetics v. 86 (6): p. 721-730; 1993 Jul. Includes
references.
Li, X.Q.; Liu, C.N.; Ritchie, S.W.; Peng, J.Y.; Gelvin, S.B.; Hodges, T.K.
Dordrecht : Kluwer Academic Publishers; 1992 Dec.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 20 (6): p. 1032-1048; 1992 Dec.
Includes references.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Nov.
Plant physiology v. 103 (3): p. 855-861; 1993 Nov. Includes references.
Daniell, H.
New York : Academic Press, 1955-; 1993.
Methods in enzymology v. 217: p. 536-556; 1993. In the series analytic:
Recombinant DNA (Part H) / edited by R. Wu. Includes references.
Rogers, H.J.; Greenland, A.J.; Hussey, P.J.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers in
association with the Society for Experimental Biology, c1991-; 1993 Nov.
The Plant journal : for cell and molecular biology v. 4 (5): p. 875-882; 1993
Nov. Includes references.
Kawasaki, T.; Hayashida, N.; Baba, T.; Shinozaki, K.; Shimada, H.
Amsterdam : Elsevier Science Publishers; 1993.
Gene v. 129 (2): p. 183-189; 1993. Includes references.
Dordrecht : Kluwer Academic Publishers; 1993 Jan.
Plant molecular biology : an international journal on molecular biology,
biochemistry and genetic engineering v. 21 (2): p. 239-248; 1993 Jan.
Includes references.
Mendel, R.R.; Clauss, E.; Schulze, J.; Steinbiss, H.H.; Nerlich, A.
Boca Raton : CRC Press; 1992.
Plant biotechnology and development / editor, Peter M. Gresshoff. p. 117-121;
1992. (A CRC series of current topics in plant molecular biology). Includes
references.
Dupuis, I.; Pace, G.M.
Berlin, W. Ger. : Springer International; 1993.
Plant cell reports v. 12 (11): p. 607-611; 1993. Includes references.
Hughes, M.A.; Dunn, M.A.; Zhang, L.; Pearce, R.S.; Goddard, N.J.; White, A.J.
Wellesbourne, Warwick : The Association of Applied Biologists; 1993.
Aspects of applied biology / (34): p. 163-171; 1993. In the series analytic:
Physiology of varieties / edited by E. White, P.S. Kettlewell, M.A. Parry, and
R.P. Ellis. Includes references.
St. Paul, Minn. : American Association of Cereal Chemists; 1992 Aug.
Cereal foods world v. 37 (8): p. 640-642; 1992 Aug. Includes references.
Quarrie, S.A.; Steed, A.; Lazic-Jancic, V.; Kovacevic, D.
Dordrecht : Kluwer Academic Publishers; 1992.
Current plant science and biotechnology in agriculture v. 13: p. 770-777;
1992. In the series analytic: Progress in plant growth regulation / edited by
C.M. Karssen, L.C. Van Loon and D. Vreugdenhil. Proceedings of the 14th
International Conference on Plant Growth Substances held July 21-26, 1991,
Amsterdam, Netherlands. Includes references.
Cejudo, F.J.; Murphy, G.; Chinoy, C.; Baulcombe, D.C.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992
Nov.
The plant journal v. 2 (6): p. 937-948; 1992 Nov. Includes references.
Gubler, F.; Jacobensen, J.V.
Rockville, Md. : American Society of Plant Physiologists; 1992 Nov.
The Plant cell v. 4 (11): p. 1435-1441; 1992 Nov. Includes references.
Sugiharto, B.; Suzuki, I.; Burnell, J.N.; Sugiyama, T.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Dec.
Plant physiology v. 100 (4): p. 2066-2070; 1992 Dec. Includes references.