Gene Expression in Oilseed, Fiber and Forage Crops

TITLE: Gene Expression in Oilseed, Fiber and Forage Crops
PUBLICATION DATE: August, 1994
ENTRY DATE: August, 1994
EXPIRATION DATE: None
UPDATE FREQUENCY: As needed
CONTACT: Biotechnology Information Center(biotech@nalusda.gov)
National Agricultural Library
DOCUMENT TYPE: Text
DOCUMENT SIZE: 326k, approx. 181 pp.

United States Department of Agriculture National Agricultural Library
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Gene Expression in Oilseed, Fiber and Forage Crops Jan 1992 - May 1994

QB 94-48
Quick Bibliographies

Ray Dobert

Gene Expression in Oilseed, Fiber and Forage Crops

SEARCH STRATEGY

SET ITEMS DESCRIPTION

      S1 872   (EXPRESS?(3W)(GENE OR GENES))/TI
      S29327   GENE()EXPRESS?/DE
      S320326  COTTON OR FLAX OR KENAF OR (FIBER()CROP?)
      S48327   GOSSYPIUM OR LINUM OR HIBISCUS
      S522922  S3 OR S4
      S69568   S1 OR S2
      S7  55   S5 AND S6
      S851813  SOYBEAN? OR SOYABEAN? OR COTTON OR CANOLA OR
               RAPE OR  SUNFLOWER? OR CRAMBE OR PEANUT? OR
               SAFFLOWER? OR (OIL OR OILSEED)()CROP?

      S914075  GLYCINE()MAX OR BRASSICA()CAMPESTRIS OR 
                    HELIANTHUS()ANNUS  OR CARTHAMUS()TINCTORIUS
OR             ARACHIS()HYPOGAEA

     S1055494  S8 OR S9
     S1118710  S5 AND S10
     S12 435   S6 AND S10
     S1337185  (FORAGE OR FODDER OR PASTURE)()CROP? OR ALFALFA OR
               CLOVER OR LUPINE? OR FESCUE OR BROMEGRASS? OR
               SUDAN()GRASS? OR TREFOIL OR SAINFOIN OR GRASS?

     S1410567  MEDICAGO OR LUPINUS OR ASTRAGALUS OR CORONILLA    
               OR CROTALARIA OR HEDYSARUM OR LABLAB OR 
               TRIGONELLA OR VICIA

     S1543854  S13 OR S14
     S16 237   S6 AND S15
     S17 682   S7 OR S12 OR S16
     S18 251   S17 AND PY=1992:1994
1                                                    NAL Call. No.: QK725.P532

A 62-kD sucrose binding protein is expressed and localized in tissues actively engaged in sucrose transport.
Grimes, H.D.; Overvoorde, P.J.; Ripp, K.; Franceschi, V.R.; Hitz, W.D. Rockville, Md. : American Society of Plant Physiologists; 1992 Dec. The Plant cell v. 4 (12): p. 1561-1574; 1992 Dec. Includes references.

Language: English

Descriptors: Glycine max; Structural genes; Plant proteins; Sucrose; Binding proteins; Dna; Nucleotide sequences; Amino acid sequences; Active transport; Plasma membranes; Mesophyll; Phloem companion cells; Cotyledons; Gene expression; Messenger RNA

Abstract: Sucrose transport from the apoplasm, across the plasma membrane, and into the symplast is critical for growth and development in most plant species. Phloem loading, the process of transporting sucrose against a concentration gradient into the phloem, is an essential first step in long-distance transport of sucrose and carbon partitioning. We report here that a soybean 62-kD sucrose binding protein is associated with the plasma membrane of several cell types engaged in sucrose transport, including the mesophyll cells of young sink leaves, the companion cells of mature phloem, and the cells of the developing cotyledons. Furthermore, the temporal expression of the gene and the accumulation pattern of the protein closely parallel the rate of sucrose uptake in the cotyledon. Molecular cloning and sequence analysis of a full-length cDNA for this 62-kD sucrose binding protein indicated that the protein is not an invertase, contains a 29-amino acid leader peptide that is absent from the mature protein, and is not an integral membrane protein. We conclude that the 62-kD sucrose binding protein is involved in sucrose transport, but is not performing this function independently.

2 NAL Call. No.: QK710.P62 Accumulation of a Brazil nut albumin in seeds of transgenic canola results in enhanced levels of seed protein methionine. Altenbach, S.B.; Kuo, C.C.; Staraci, L.C.; Pearson, K.W.; Wainwright, C.; Georgescu, A.; Townsend, J.
Dordrecht : Kluwer Academic Publishers; 1992 Jan. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (2): p. 235-245; 1992 Jan. Includes references.

Language: English

Descriptors: Bertholletia excelsa; Brassica napus; Gene transfer; Genetic transformation; Transgenics; Albumins; Genes; Chimeras; Gene expression; Seeds; Methionine; Plant proteins; Protein value; Seed development; Amino acids

Abstract: We have increased the methionine content of the seed proteins of a commercial winter variety of canola-rich seed protein from Brazil nut in the seeds of by expressing a chimeric gene encoding a methionine-rich seed protein from Brazil nut in the seeds of transgenic plants. Transgenic canola seeds accumulate the heterologous methionine-rich protein at levels which range from 1.7% to 4.0% of the total seed protein and contain up to 33% more methionine. The precursor of the methionine-rich protein is processed correctly in the seeds, resulting in the appearance of the mature protein in the 2S protein fraction. The 2S methionine-rich protein accumulates in the transgenic seeds at the same time in development as the canola 11S seed proteins and disappears rapidly upon germination of the seed. The increase in methionine in the canola seed proteins should increase the value of canola meal which is used in animal feed formulations.

3 NAL Call. No.: QK710.A9 Acid-tolerant species of Medicago produce root exudates at low pH which induce the expression of nodulation genes in Rhizobium meliloti. Howieson, J.G.; Robson, A.D.; Abbott, L.K. East Melbourne : Commonwealth Scientific and Industrial Research Organization; 1992.
Australian journal of plant physiology v. 19 (3): p. 287-296; 1992. Includes references.

Language: English

Descriptors: Medicago; Medicago polymorpha; Medicago truncatula; Medicago littoralis; Rhizobium meliloti; Rhizobium leguminosarum; Escherichia coli; Symbiosis; Root nodules; Nodulation; Genetic regulation; Plasmids; Gene expression; Transcription; Acidity; Tolerance; Ph; Root exudates; Calcium; Genes

4 NAL Call. No.: QK710.P62 Activation of flavonoid biosynthesis in roots of Vicia sativa subsp. nigra plants by inoculation with Rhizobium leguminosarum biovar viciae. Recourt, K.; Tunen, A.J. van; Mur, L.A.; Brussel, A.N.A. van; Lugtenbergh, B.J.J.; Kijne, J.W.
Dordrecht : Kluwer Academic Publishers; 1992 Jun. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (3): p. 411-420; 1992 Jun. Includes references.

Language: English

Descriptors: Vicia sativa subsp. nigra; Rhizobium leguminosarum; Roots; Infection; Phenylalanine ammonia-lyase; Transferases; Naringenin-chalcone synthase; Enzyme activity; Bacterial proteins; Gene expression; Messenger RNA; Nodulation; Flavonoids; Biosynthesis

Abstract: Infective (nodulating) Rhizobium leguminosarum biovar viciae (R.l. viciae) bacteria release Nod factors which stimulate the release of nodulation gene-inducing flavanones and chalcones from roots of the host plant Vicia sativa subsp. nigra (K. Recourt et al., Plant Mol Biol 16: 841-852; H.P. Spaink et al., Nature 354: 125-130). The hypothesis that this release results from increased synthesis of flavonoids was tested by studying the effect of inoculation of V. sativa with infective and uninfective R.l. viciae bacteria on (i) activity of L-phenylalanine ammonia-lyase, (ii) level of chalcone synthase mRNA, and (iii) activity of (eriodictyol) methyltransferase in roots. Consistent with the hypothesis, each of these parameters was found to increase 1.5 to 2-fold upon inoculation with infective R.l. viciae bacteria relative to the situation for uninoculated roots and for roots inoculated with uninfective rhizobia.

5 NAL Call. No.: QK710.P62 Activation of flavonoid biosynthesis in roots of Vicia sativa subsp. nigra plants by inoculation with Rhizobium leguminosarum biovar viciae. Recourt, K.; Tunen, A.J. van; Mur, L.A.; Brussel, A.N.A. van; Lugtenbergh, B.J.J.; Kijne, J.W.
Dordrecht : Kluwer Academic Publishers; 1992 Jun. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (3): p. 411-420; 1992 Jun. Includes references.

Language: English

6 NAL Call. No.: QK710.P62 The activation process of Arabidopsis thaliana A1 gene encoding the translation elongation factor EF-1 alpha conserved among angiosperms. Curie, C.; Liboz, T.; Montane, M.H.; Rouan, D.; Axelos, M.; Lescure, B. Dordrecht : Kluwer Academic Publishers; 1992 Apr. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (6): p. 1083-1089; 1992 Apr. Includes references.

Language: English

Descriptors: Arabidopsis thaliana; Nicotiana tabacum; Zea mays; Brassica campestris; Lycopersicon esculentum; Multigene families; Translation; Proteins; Introns; Controlling elements; Promoters; Mutations; Dna binding proteins; Evolution; Transgenics; Genetic transformation; Gene expression; Transcription; Nucleotide sequences

Abstract: In Arabidopsis thaliana, the activation process of the A1 EF-1 alpha gene depends on several elements. Using the GUS reporter gene, transient expression experiments have shown that mutations of upstream cis-acting elements of the A1 promoter, or the deletion of an intron located within the 5' non-coding region, similarly affect expression in dicot or monocot protoplasts. The results reported here strongly suggest that this 5' intron is properly spliced in Zea mays. We show that two trans-acting factors, specifically interacting with an upstream activating sequence (the TEF 1 box), are present in nuclear extracts prepared from A. thaliana, Brassica rapa, Nicotiana tabacum and Z. mays. In addition, a DNA sequence homologous to the TEF 1 box, found at approximately the same location within a Lycopersicon esculentum EF-1 alpha promoter, interacts with the same trans-acting factors. Homologies found between the A. thaliana and L. esculentum TEF 1 box sequences have allowed us to define mutations of this upstream element which affect the interaction with the corresponding trans-acting factors. These results support the notion that the activation processes of A. thaliana EF-1 alpha genes have been conserved among angiosperms and provide interesting data on the functional structure of the TEF 1 box.

7 NAL Call. No.: QK710.P68 Active cdc2 genes and cell cycle phase-specific cdc2-related kinase complexes in hormone-stimulated alfalfa cells.
Magyar, Z.; Bako, L.; Bogre, L.; Dedeoglu, D.; Kapros, T.; Dudits, D. Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993 Jul.
The plant journal v. 4 (1): p. 151-161; 1993 Jul. Includes references.

Language: English

Descriptors: Medicago sativa; Structural genes; Protein kinase; Transcription; Gene expression; Messenger RNA; Cell suspensions; Mesophyll; Protoplasts; Roots; Genetic regulation; Cell division; 2,4-d; Naa; Zeatin riboside; Callus; Enzyme activity; Histones; Phosphorylation

8 NAL Call. No.: 23 AU792 The adaptation of Medicago polymorpha to a range of edaphic and environmental conditions: effect of temperature on growth, and acidity stress on nodulation and nod gene induction.
Loi, A.; Howieson, J.G.; Cocks, P.S.; Caredda, S. East Melbourne : Commonwealth Scientific and Industrial Research Organization; 1993.
Australian journal of experimental agriculture v. 33 (1): p. 25-30; 1993. Includes references.

Language: English

Descriptors: Sardinia; Medicago polymorpha; Genotypes; Adaptation; Edaphic factors; Environmental factors; Growth; Nodulation; Rhizobium meliloti; Gene expression; Soil acidity; Stress

9 NAL Call. No.: QK725.P54 Agrobacterium tumefaciens-mediated beta-glucuronidase (GUS) gene expression in lentil (Lens culinaris Medik.) tissues. Warkentin, T.D.; McHughen, A.
Berlin, W. Ger. : Springer International; 1992. Plant cell reports v. 11 (5/6): p. 274-278; 1992. Includes references.

Language: English

Descriptors: Lens culinaris; Beta-glucuronidase; Gene expression; Genetic transformation; Agrobacterium tumefaciens; Extracts; In vitro culture

Abstract: Lentil (Lens culinaris Medik.) shoot apex, epicotyl, and root explants were capable of expressing an intron-containing beta-glucuronidase (GUS) gene after inoculation with the disarmed Agrobacterium strain GV2260:p35SGUSINT. Expression occurred at all wound sites on these explants except at the end of the root explants proximal to the cotyledonary node. GUS expression was detected using both histochemical and fluorescence assays and was stable for at least nine days after inoculation for epicotyl and root explants, and for at least seventeen days for shoot apices. Non-inoculated controls, or controls inoculated with an Agrobacterium strain lacking the GUS gene, did not produce any background blue staining in the histochemical assay. Expression levels for all lentil explants were substantially lower than for comparable flax (Linum usitatissimum L.) explants which served as a positive control.

10 NAL Call. No.: QK725.P54 Agrobacterium tumefaciens-mediated transformation of safflower (Carthamus tinctorius L.) cv. 'Centennial'.
Ying, M.C.; Dyer, W.E.; Bergman, J.W.
Berlin, W. Ger. : Springer International; 1992. Plant cell reports v. 11 (11): p. 581-585; 1992. Includes references.

Language: English

Descriptors: Carthamus tinctorius; Agrobacterium tumefaciens; Genetic transformation; Explants; Callus; Regenerative ability; Shoots; Buds; Gene expression; Beta-glucuronidase; Reporter genes; Culture media; Laboratory methods

Abstract: Efficient callus formation was achieved from cotyledon, stem, and leaf explants of the domestic safflower cultivar 'Centennial' on MS salts medium containing 1 mg/L BAP and 1 mg/L NAA. Shoot buds were regenerated from 26% of leaf-derived calli on callus induction medium, although attempts to root regenerated shoots were not successful. 'Centennial' explants inoculated with Agrobacterium tumefaciens containing NPT II and GUS genes produced kanamycin-resistant calli from which buds were regenerated. Transformation and stable integration of transgenes was confirmed by GUS assay and DNA hybridization in kanamycin-resistant calli, and GUS assay in regenerated shoots.

11 NAL Call. No.: QK710.P63 Agrobacterium-mediated transformation of kenaf (Hibiscus cannabinus L.) with the beta-glucuronidase (GUS) gene.
Banks, S.W.; Gossett, D.R.; Lucas, M.C.; Milhollon, E.P.; LaCelle, M.G. Athens, Ga. : International Society for Plant Molecular Biology, University of Georgia; 1993 Jun.
Plant molecular biology reporter - ISPMB v. 11 (2): p. 101-104; 1993 Jun. Includes references.

Language: English

Descriptors: Hibiscus cannabinus; Agrobacterium; Genetic transformation; Gene transfer; Beta-glucuronidase; Genetic code; Tissue culture; Regenerative ability; Enzyme activity; Gene expression

12 NAL Call. No.: QK725.P532 Alfalfa cyclins: differential expression during the cell cycle and in plant organs.
Hirt, H.; Mink, M.; Pfosser, M.; Bogre, L.; Gyorgyey, J.; Jonak, C.; Gartner, A.; Dudits, D.; Heberle-Bors, E.
Rockville, Md. : American Society of Plant Physiologists; 1992 Dec. The Plant cell v. 4 (12): p. 1531-1538; 1992 Dec. Includes references.

Language: English

Descriptors: Medicago sativa; Medicago varia; Structural genes; Dna; Plant proteins; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Cell division; Leaves; Roots; Stems; Flowers; Buds

Abstract: Cell division in eukaryotes is mediated by the action of the mitosis promoting factor, which is composed of the CDC2 protein kinase and one of the various mitotic cyclins. We have recently isolated a cdc2 gene from alfalfa. Here, we report the isolation of two cyclin genes, cycMs1 and cycMs2, from alfalfa. The cycMs2 gene shows highest similarity to type B cyclins. In contrast, the predicted amino acid sequence of the cycMs1 gene shows similar homology scores to cyclins of all types (25 to 35%). Both genes are expressed in dividing suspension cultured cells but cease to be expressed when the cells enter stationary phase. In synchronized alfalfa suspension cultured cells, the mRNAs of cycMs1 and cycMs2 show maximal expression in the G2 and M phases. Transcripts of cycMs2 are found only in late G2 and M phase cells, an expression pattern typical for cyclin B genes, whereas cycMs1 appears with the onset of G2. This pattern indicates that alfalfa cycMs1 and cycMs2 belong to different classes of cyclins. In young leaves, expression of both genes is high, whereas in mature leaves no transcripts can be detected, indicating that the two cyclin genes are true cell division markers at the mRNA level. In other organs, a more complex expression pattern of the two cyclin genes was found.

13 NAL Call. No.: QK710.P62 Alfalfa root nodule phosphoenolpyruvate carboxylase: characterization of the cDNA and expression in effective and plant-controlled ineffective nodules. Pathirana, S.M.; Vance, C.P.; Miller, S.S.; Gantt, J.S. Dordrecht : Kluwer Academic Publishers; 1992 Nov. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 20 (3): p. 437-450; 1992 Nov. Includes references.

Language: English

Descriptors: Medicago sativa; Structural genes; Dna; Multigene families; Phosphoenolpyruvate carboxylase; Nucleotide sequences; Amino acid sequences; Gene expression; Root nodules; Genetic regulation; Enzyme activity; Messenger RNA

Abstract: Phosphoenolpyruvate carboxylase (PEPC) plays a key role in N2 fixation and ammonia assimilation in legume root nodules. The enzyme can comprise up to 2% of the soluble protein in root nodules. We report here the isolation and characterization of a cDNA encoding the nodule-enhanced form of PEPC. Initially, a 2945 bp partial-length cDNA was selected by screening an effective alfalfa nodule cDNA library with antibodies prepared against root nodule PEPC. The nucleotide sequence encoding the N-terminal region of the protein was obtained by primer-extension cDNA synthesis and PCR amplification. The complete amino acid sequence of alfalfa PEPC was deduced from these cDNA sequences and shown to bear striking similarity to other plant PEPCs. Southern blots of alfalfa genomic DNA indicate that nodule PEPC is a member of a small gene family. During the development of effective root nodules, nodule PEPC activity increases to a level that is 10- to 15-fold greater than that in root and leaf tissue. This increase appears to be the result of increases in amount of enzyme protein and PEPC mRNA. Ineffective nodules have substantially less PEPC mRNA, enzyme protein and activity than do effective nodules. Maximum expression of root nodule PEPC appears to be related to two signals. The first signal is associated with nodule initiation while the second signal is associated with nodule effectiveness. Regulation of root nodule PEPC activity may also involve post-translational processes affecting enzyme activity and/or degradation.

14 NAL Call. No.: 442.8 D49 Altered morphology in transgenic tobacco plants that overproduce cytokinins in specific tissues and organs.
Li, Y.; Hagen, G.; Guilfoyle, T.J.
Orlando, Fla. : Academic Press; 1992 Oct. Developmental biology v. 153 (2): p. 386-395; 1992 Oct. Includes references.

Language: English

Descriptors: Nicotiana tabacum; Cytokinins; Transgenics; Genetic transformation; Escherichia coli; Agrobacterium tumefaciens; Beta-glucuronidase; Reporter genes; Promoters; Genes; Gene expression; Plant morphology; Plant development; Plant tissues; Plant organs; Histochemistry

Abstract: An auxin-inducible bidirectional promoter from the soybean SAUR gene locus was fused to a reporter gene in one direction and a cytokinin biosynthetic gene in the opposite direction and the expression of these fused genes was examined in transgenic tobacco. The Escherichia coli uidA gene, which encodes the enzyme beta-glucuronidase (GUS), was used as the reporter gene and the Agrobacterium tumefaciens ipt gene, which encodes the enzyme isopentenyl transferase, was used as the cytokinin biosynthetic gene. These constructs allowed the overproduction of cytokinins in tobacco in a tissueand organ-specific manner. Localized overproduction of cytokinins was monitored using the GUS reporter gene and measured by an ELISA assay. The tissue- and organ-specific overproduction of cytokinins produced a number of morphological and physiological changes, including stunting, loss of apical dominance, reduction in root initiation and growth, either acceleration or prolonged delayed senescence in leaves depending on the growth conditions, adventitious shoot formation from unwounded leaf veins and petioles, altered nutrient distribution, and abnormal tissue development in stems. While some of these morphological changes result directly from the localized overproduction of cytokinins, other changes probably result from the mobilization of plant nutrients to tissues rich in cytokinins.

15 NAL Call. No.: 450 P692 Appearance of new lipoxygenases in soybean cotyledons after germination and evidence for expression of a major new lipoxygenase gene. Kato, T.; Ohta, H.; Tanaka, K.; Shibata, D. Rockville, Md. : American Society of Plant Physiologists; 1992 Jan. Plant physiology v. 98 (1): p. 324-330; 1992 Jan. Includes references.

Language: English

Descriptors: Glycine max; Cotyledons; Plant composition; Lipoxygenase; Seed germination; Genetic regulation; Gene expression; Genetic code; Amino acid sequences

Abstract: The appearance and subsequent disappearance of lipoxygenase activity at pH 6.8 in germinated cotyledons of soybean (Glycine max [L.]) was shown using a variant soybean cultivar (Kanto 101) that lacks the two lipoxygenase isozymes, L-2 and L-3, that are present in dry seeds of a normal soybean cultivar (Enrei). Three new lipoxygenases, designated lipoxygenase L-4, L-5, and L-6, were purified using anionic or cationic ion exchange chromatography. The major lipoxygenase in 5-day-old cotyledons of the variant soybean was lipoxygenase L-4. Lipoxygenases L-5 and L-6 preferentially produced 13(S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid (13S-HPOD) as a reaction product of linoleic acid, whereas lipoxygenase L-4 produced both 13S-HPOD and 9(S)-hydroperoxy-10(E),12(Z)-octadecadienoic acid. All three isozymes have pH optima of 6.5, no activity at pH 9.0, and preferred linolenic acid to linoleic acid as a substrate. Partial amino acid sequencing of lipoxygenase L-4 showed that this isozyme shares amino acid sequence homology with lipoxygenases L-1, L-2, and L-3 but is not identical to any of them. This indicates that a new lipoxygenase, L-4, is expressed in cotyledons.

16 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).

17 NAL Call. No.: QK710.A9 Auxin-regulated transcription.
Guilfoyle, T.J.; Hagen, G.; Li, Y.; Ulmasov, T.; Liu, Z.; Strabala, T.; Gee, M.
Melbourne, Commonwealth Scientific and Industrial Research Organization; 1993. Australian journal of plant physiology v. 20 (4/5): p. 489-502; 1993. Includes references.

Language: English

Descriptors: Arabidopsis; Glycine max; Auxins; Amino acid sequences; Beta-glucuronidase; Cytokinins; Gene expression; Messenger RNA; Plant development; Plant physiology; Transcription

18 NAL Call. No.: QK1.B38 Bacterial-induced changes in plant form and function. Hirsch, A.M.; McKhann, H.I.; Lobler, M. Chicago, Ill. : University of Chicago Press; 1992 Sep. International journal of plant sciences v. 153 (3,pt.2): p. S171-S181; 1992 Sep. Paper presented at the "Katherine Esau Symposium on Plant Structure: Concepts, Connection and Challenges," March 28-31, 1992, Davis, California. Includes references.

Language: English

Descriptors: Medicago sativa; Rhizobium meliloti; Agrobacterium tumefaciens; Roots; Root hairs; Root nodules; Nodulation; Cell differentiation; Nitrogen fixation; Gene expression; Meristems; Mutants; Recombinant DNA; Genetic transformation

19 NAL Call. No.: QK710.P68 cdc2MsB, a cognate cdc2 gene from alfalfa, complements the G1/S but not the G2/M transition of budding yeast cdc28 mutants. Hirt, H.; Pay, A.; Bogre, L.; Meskiene, I.; Heberle-Bors, E. Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993 Jul.
The plant journal v. 4 (1): p. 61-69; 1993 Jul. Includes references.

Language: English

Descriptors: Medicago sativa; Saccharomyces cerevisiae; Complementary DNA; Structural genes; Protein kinase; Nucleotide sequences; Amino acid sequences; Complementation; Mutants; Gene expression; Messenger RNA; Cell division

20 NAL Call. No.: QK710.P62 cDNA sequence and expression of a phosphoenolpyruvate carboxylase gene from soybean.
Sugimoto, T.; Kawasaki, T.; Kato, T.; Whittier, R.F.; Shibata, D.; Kawamura, Y.
Dordrecht : Kluwer Academic Publishers; 1992 Nov. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 20 (4): p. 743-747; 1992 Nov. Includes references.

Language: English

Descriptors: Glycine max; Structural genes; Phosphoenolpyruvate carboxylase; Dna; Nucleotide sequences; Amino acid sequences; Gene expression; Leaves; Stems; Roots; Seeds; Messenger RNA

Abstract: A full-length cDNA encoding a subunit of phosphoenolpyruvate carboxylase (PEPC) was isolated from a developing seed expression library of the C3 plant Glycine max. The corresponding mRNA is present at similar levels in leaf, stem, root and developing seed. Two potential start codons exist, and the activity of protein initiated from the first such codon could be subject to regulation by protein kinase. Sequence comparison shows a similar upstream start codon in the case of the Ppc2 gene from Mesembryanthemum crystallinum, previously assumed to lack the sequences necessary for phosphorylation. The soybean encoded protein tends to resemble other 'C3-type' PEPC proteins more closely than those implicated in C4 or crassulacean acid metabolism.

21 NAL Call. No.: 450 P692 cDNA sequence, expression, and transcript stability of a cold acclimation-specific gene, cas18, of alfalfa (Medicago falcata) cells. Wolfraim, L.A.; Langis, R.; Tyson, H.; Dhindsa, R.S. Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Apr. Plant physiology v. 101 (4): p. 1275-1282; 1993 Apr. Includes references.

Language: English

Descriptors: Medicago falcata; Complementary DNA; Structural genes; Nucleotide sequences; Amino acid sequences; Plant proteins; Cold; Acclimatization; Gene expression; Messenger RNA; Cell suspensions; Genetic regulation

Abstract: The nucleotide sequence of a full-length cDNA, the deduced amino acid sequence, and the regulation of expression of a cold acclimation-specific gene, cas18, in cell suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago falcata cv Anik) have been determined. The deduced polypeptide, CAS18, is relatively small (17.6 kD), is highly hydrophilic, is rich in glycine and threonine, and contains two distinctive repeat elements. It exhibits homology with members of the LEA/RAB/dehydrin family of proteins, which accumulate in response to abscisic acid (ABA) or water stress. It is intriguing that cas18 is induced by neither ABA nor water stress. The cas18 cDNA hybridizes to three transcripts of 1.6, 1.4, and 1.0 kb, and the cDNA characterized here corresponds to the 1.0-kb transcript. The expression of this gene is about 30-fold greater in cold-acclimated cells than in nonacclimated cells. Although the accumulation of transcripts during cold acclimation is relatively slow, their disappearance during deacclimation is dramatically rapid, becoming undetectable in less than 5 h. Studies of nuclear run-on transcription show that cold acclimation enhances the transcription of this gene nearly 9-fold. The stability of cas18 -detectable transcripts during deacclimation is considerably increased if transcription is inhibited with cordycepin. It therefore appears that low temperature regulates the expression of cas18 at both the transcriptional and posttranscriptional levels.

22 NAL Call. No.: QK710.P62 cDNA sequence of a sunflower oleosin and transcript tissue specificity. Cummins, I.; Murphy, D.J.
Dordrecht : Kluwer Academic Publishers; 1992 Aug. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (5): p. 873-876; 1992 Aug. Includes references.

Language: English

Descriptors: Helianthus annuus; Structural genes; Plant proteins; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Plant embryos; Seeds

Abstract: Oleosins (oil body membrane proteins) of 20.5 and 18 kDa have been purified from sunflower (Helianthus annuus) seeds and polyclonal antibodies raised against them. The precipitated rabbit immunoglobulin fraction was purified by affinity chromatography on cyanogen bromide-activated Sepharose and specifically recognised polypeptides of 18 and 20.5 kDa in sunflower homogenate and oil body fractions assayed by western blotting. A near-full-length cDNA clone was isolated for the 20.5 kDa oleosin. The 694 bp cDNA contained an open reading frame of 534 bp, followed by an untranslated region of 81 bp and a poly(A) region of 70 bp. The open reading frame encoded a polypeptide of 19.8 kDa. Study of transcript localisation revealed message to be abundant in the embryo during the later stage of development and still present in the dry seed. No signal was observed in RNA prepared from expanding leaves.

23 NAL Call. No.: 450 J8224 Changes in levels of gene trasncripts and their corresponding proteins in nodules of soybean plants subjected to dark-induced stress. Gordon, A.J.; Ougham, H.J.; James, C.L. Oxford : Oxford University Press; 1993 Sep. Journal of experimental botany v. 44 (266): p. 1453-1460; 1993 Sep. Includes references.

Language: English

Descriptors: Glycine max; Messenger RNA; Gene expression; Root nodules; Leghemoglobin; Glutamate-ammonia ligase; Sucrose synthase; Enzyme activity; Dark; Stress

Abstract: Experiments were carried out to investigate the effects of stress on the levels and activities of key nodule proteins and the amounts of the mRNAs encoding these proteins. Soybean plants, subjected to 3 d of continuous darkness and then returned to the normal light/dark regime, were used as a model system. Samples of nodules were taken during the stress/recovery cycle and total RNA and total soluble protein were extracted. The levels of mRNAs encoding leghaemoglobin (Lb), sucrose synthase (SS) and glutamine synthetase (GS) were estimated using Northern and slot blots. Within 24 h of complete darkness the levels of all three transcripts had fallen significantly (by 90%, 70% and 50% for SS, Lb and GS mRNAs, respectively) and continued to decline for the next 2 d of darkness. When the plants were returned to the normal light/dark regime, all transcript levels rapidly increased again. The corresponding proteins were analysed for biological activity (enzyme activities in the cases of SS and GS, and haem content for Lb) and amount of protein (using Western blotting and specific antibodies raised against Lb, SS and GS). The amounts and activities of Lb and GS were unchanged, whilst those of SS declined significantly over the 3 d dark period and increased again during the period following return to the normal light/dark regime. Neither the imposition of a 30 min light break each 24 h during the continuous dark treatments, nor the addition of 50 mol m-3 sucrose to the daily supply of nutrients had any effect on the changes described.

24 NAL Call. No.: SB732.6.M65 Characterization of a chimeric cauliflower mosaic virus isolate that is more severe and accumulates to higher concentrations than either of the strains from which it was derived.
Anderson, E.J.; Trese, A.T.; Sehgal, O.P.; Schoelz, J.E. St. Paul, Minn. : APS Press; 1992 Jan.
Molecular plant-microbe interactions : MPMI v. 5 (1): p. 48-54; 1992 Jan. Includes references.

Language: English

Descriptors: Brassica campestris var. rapa; Cauliflower mosaic caulimovirus; Strains; Strain differences; Virulence; Dwarfing; Symptoms; Chimeras; Phenotypes; Viral antigens; Genes; Gene expression; Dna; Rna; Genetic analysis; Stability; Synergism; Molecular biology

25 NAL Call. No.: QK710.P62 Characterization of a Gy4 glycinin gene from soybean Glycine max cv. Forrest. Xue, Z.T.; Xu, X.L.; Shen, W.; Zhuang, N.L.; Hu, W.H.; Shen, S.C. Dordrecht : Kluwer Academic Publishers; 1992 Mar. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (5): p. 897-908; 1992 Mar. Includes references.

Language: English

Descriptors: Glycine max; Multigene families; Plant proteins; Nucleotide sequences; Amino acid sequences; Molecular conformation; Exons; Introns; Cultivars; Transposable elements; Repetitive DNA; Restriction mapping; Gene expression; Messenger RNA

Abstract: The glycinin gene family encoding the glycinin subunits in soybean plants is composed of at least five gene members. A genomic clone lambda S312 containing the Gy4 gene from a genomic library of cv. Forrest was isolated and partially characterized. The organization of this gene was found to be similar to that of a null allele from cv. Raiden, but different from the Gy4 gene from cv. Dare. The complete nucleotide sequence of this gene has been determined. It is 2599 bp long consisting of four exons and three introns. Comparing the DNA sequences between this gene and the gene from Dare and a null allele from Raiden, the difference found in the coding region was 5'-GCAGTGCAAG-3' (nt 824 to 833) in the former case versus 5'-TGGAGTTGCAATT-3' (nt 1314 to 1326) in the latter case in the exon 2 domain, resulting in three amino acid differences and one amino acid absence. Some other differences were also found in the non-coding region. The coding sequence and 5'-flanking region of the Gy4 gene, when compared with that of other legumin genes as well as group 1 glycinin subunit genes, revealed some interesting features: (1) a transposable element-like sequence was found in the hypervariable region (HVR) of the exon 3 domain, which was lacking in the legumin and the glycinin group 1 genes; (2) in the 5'-flanking region from nt -145 to -1, two high-homology sequences were found: one from nt -141 to nt -132, the other from nt -118 to nt -92 which includes the 'legumin box' and the RY repeat element.

26 NAL Call. No.: 450 P692 Characterization of a novel protein induced by progressive or rapid drought and salinity in Brassica napus leaves.
Reviron, M.P.; Vartanian, N.; Sallantin, M.; Huet, J.C.; Pernollet, J.C.; Vienne, D. de
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov. Plant physiology v. 100 (3): p. 1486-1493; 1992 Nov. Includes references.

Language: English

Descriptors: Brassica napus var. oleifera; Plant proteins; Leaves; Water stress; Drought; Salinity; Adaptation; Messenger RNA; Gene expression; Water deficit; Amino acid sequences

Abstract: Under progressive drought stress, Brassica napus displays differential leaf modifications. The oldest leaves, developed before the onset of water deficit, wilt gradually, whereas the youngest leaves harden. Hardening was distinguished by leaf turgor and bluish wax bloom when the shoot water potential was below -3 MPa and the leaf water saturation deficit was about 60%. This adaptive change was accompanied by modifications in two-dimensional protein profiles. Ten percent of the polypeptides had altered abundance or were unique to drought-stressed plants. Two-dimensional analysis of in vitro translation products did not reveal a general decrease in mRNA population. A 22-kD double polypeptide was increased by progressive or rapid water stress and salinity and disappeared upon rehydration. These polypeptides have a common N-terminal sequence, which does not reveal homology with any known water-stress protein but which contains the signature motif of soybean Kunitz trypsin inhibitors. Immunoprecipitation allowed these polypeptides to be identified on two-dimensional gels of in vitro translation products. They appeared to be synthesized as a 24-kD precursor, and their transcript was present in the control well-watered leaves, where the polypeptides were never detected, indicating a possible translational regulation. A putative function of this protein, named BnD22, in the retardation of drought-induced leaf senescence is discussed.

27 NAL Call. No.: QK710.P68 Characterization of a pollen-specific cDNA from sunflower encoding a zinc finger protein.
Baltz, R.; Domon, C.; Pillay, D.T.N.; Steinmetz, A. Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992 Sep.
The plant journal v. 2 (5): p. 713-721; 1992 Sep. Includes references.

Language: English

Descriptors: Helianthus annuus; Complementary DNA; Structural genes; Dna binding proteins; Nucleotide sequences; Pollen; Amino acid sequences; Introns; Multigene families; Gene expression; Messenger RNA; Zinc; Binding site

28 NAL Call. No.: QK710.P62 Characterization of a stress-induced, developmentally regulated gene family from soybean.
Crowell, D.N.; John, M.E.; Russell, D.; Amasino, R.M. Dordrecht : Kluwer Academic Publishers; 1992 Feb. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (3): p. 459-466; 1992 Feb. Includes references.

Language: English

Descriptors: Glycine max; Multigene families; Plant proteins; Gene expression; Stress; Roots; Leaves; Seedlings; Senescence; Abiotic injuries; Nucleotide sequences; Amino acid sequences

Abstract: We describe a family of stress-induced, developmentally regulated soybean genes for which cDNAs have been obtained from two different cultivars (Glycine max cv. Mandarin and Glycine max cv. Williams). The mRNAs corresponding to these cDNAs, called SAM22 and H4, respectively, accumulate predominantly in the roots of soybean seedlings but are present at high levels in the roots and leaves of mature plants. SAM22 accumulation is especially dramatic in senescent leaves. In addition, SAM22 accumulation can be induced in young leaves by wounding or by transpiration-mediated uptake of salicylic acid, methyl viologen, fungal elicitor, hydrogen peroxide or sodium phosphate (pH 6.9). Taken together, these data indicate that the genes corresponding to SAM22 and H4 are induced by various stresses and developmental cues. Southern blot analysis indicates that multiple copies of sequences related to SAM22 exist in the soybean genome. We also show that the nucleotide sequences of the cDNAs corresponding to SAM22 and H4 are 86% identical at the nucleotide level to each other and 70% identical at the amino acid level to the 'disease resistance response proteins' of Pisum sativum.

29 NAL Call. No.: QK710.P68 Characterization of GmENOD40, a gene showing novel patterns of cell-specific expression during soybean nodule development. Yang, W.C.; Katinakis, P.; Hendriks, P.; Smolders, A.; Vries, F. de; Spee, J.; Kammen, A. van; Bisseling, T.; Franssen, H. Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993 Apr.
The plant journal v. 3 (4): p. 573-585; 1993 Apr. Includes references.

Language: English

Descriptors: Glycine max; Pisum sativum; Root nodules; Ontogeny; Genetic regulation; Genetic code; Nucleotide sequences; Gene expression; Roots; Cell division; Developmental stages; Plant anatomy

30 NAL Call. No.: QH426.C8 Characterization of the Brassica campestris mitochondrial gene for subunit six of NADH dehydrogenase: nad6 is present in the mitochondrion of a wide range of flowering plants.
Nugent, J.M.; Palmer, J.D.
Berlin ; New York : Springer-Verlag, 1979-; 1993. Current genetics v. 23 (2): p. 148-153; 1993. Includes references.

Language: English

Descriptors: Brassica campestris; Plants; Structural genes; Nadh dehydrogenase; Nucleotide sequences; Amino acid sequences; Mitochondrial DNA; Rna editing; Transcription; Gene expression

Abstract: We have isolated the Brassica campestris mitochondrial gene nad6, coding for subunit six of NADH dehydrogenase. The deduced amino-acid sequence of this gene shows considerable similarity to mitochondrially encoded NAD6 proteins of other organisms as well as to NAD6 proteins coded for by plant chloroplast DNAs. The B. campestris nad6 gene appears to lack introns and produces an abundant transcript which is comparable in size to a previously described, unidentified transcript (#18) mapped to the B. campestris mitochondrial genome. An alignment of NAD6 proteins (deduced from DNA sequences) suggests that B. campestris nad6 transcripts are edited. Southern-blot hybridization indicates that nad6 is present in the mitochondrial genome of all of a wide range of flowering plant species examined.

31 NAL Call. No.: QK710.P62 Characterization of the soybean early nodulin cDNA clone GmENOD55. Blank, C. de; Mylona, P.; Yang, W.C.; Katinakis, P.; Bisseling, T.; Franssen, H.
Dordrecht : Kluwer Academic Publishers; 1993 Sep. Plant molecular biology v. 22 (6): p. 1167-1171; 1993 Sep. Includes references.

Language: English

Descriptors: Glycine max; Complementary DNA; Nodulins; Multigene families; Nucleotide sequences; Amino acid sequences; Gene expression; Genetic regulation; Nodulation; Bradyrhizobium japonicum; Rhizobium

Abstract: Two cDNA clones of the soybean early nodulin GmENOD55 were characterized. These clones may represent two members of the soybean early nodulin gene family GmENOD55. GmENOD55 has an N-terminal signal peptide and it contains an internal domain consisting of proline and serine residues. Analyses of nodules lacking infection threads and intracellular bacteria suggest that the GmENOD55 gene is first expressed after release of Bradyrhizobium japonicum in plant cells. This conclusion is supported by in situ hybridization studies showing that the expression is restricted to the infected cell type.

32 NAL Call. No.: 450 P693 Chitinase and peroxidase in effective (fix+) and ineffective (fix-) soybean nodules.
Staehelin, C.; Muller, J.; Mellor, R.B.; Wiemken, A.; Boller, T. Berlin : Springer-Verlag; 1992.
Planta v. 187 (3): p. 295-300; 1992. Includes references.

Language: English

Descriptors: Glycine max; Bradyrhizobium japonicum; Cortex; Roots; Root nodules; Plant composition; Chitinase; Peroxidase; Symbiosis; Disease resistance; Gene expression; Plant pathogens

Abstract: Chitinase and peroxidase, two enzymes thought to be involved in the defense of plants against pathogens, were measured in soybean (Glycine max L. Merr.) roots and in nodules colonized by Bradyrhizobium japonicum strains differing in their symbiotic potential. Activities of both enzymes were higher in nodules than in roots. In "effective", nitrogen-fixing nodules, colonized by wild-type bacteria, chitinase and peroxidase activities had low levels in the central infected zone and were enhanced primarily in the nodule cortex. An ascorbate-specific peroxidase, possibly involved in radical scavenging, had similarly high activities in the infected zone and in the cortex. "Ineffective" nodules colonized by bacteria unable to fix nitrogen symbiotically showed a similar distribution of chitinase and peroxidase. In another type of "ineffective" nodule, colonized by a B. japonicum strain eliciting a hypersensitive response, activities of both enzymes were enhanced to a similar degree in the infected zone as well as in the cortex. Tissue prints using a direct assay for peroxidase and an antiserum against bean chitinase corroborated these results. The antiserum against bean chitinase cross-reacted with a nodule protein of Mr 32 000; it inhibited most of the chitinase activity in the nodules but barely affected the chitinase in uninfected roots. It is concluded that proteins characteristic of the defense reaction accumulate in the cortex of nodules independently of their ability to fix nitrogen, and in the entire body of hypersensitively reacting nodules.

33 NAL Call. No.: 450 P692 Chlorophyll a/b-binding protein gene expression in cotton. Anderson, D.M.; Hudspeth, R.L.; Hobbs, S.L.; Grula, J.W. Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul. Plant physiology v. 102(3): p. 1047-1048; 1993 Jul. Includes references.

Language: English

Descriptors: Gossypium hirsutum; Structural genes; Chlorophyll a/b binding protein; Gene expression; Messenger RNA; Nucleotide sequences; Amino acid sequences; Leaves; Stems; Promoters; Recombinant DNA; Reporter genes; Beta-glucuronidase; Histoenzymology

34 NAL Call. No.: QK710.P62 Chlorophyll a/b-binding protein genes are differentially expressed during soybean development.
Chang, Y.C.; Walling, L.L.
Dordrecht : Kluwer Academic Publishers; 1992 May. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (2): p. 217-230; 1992 May. Includes references.

Language: English

Descriptors: Glycine max; Multigene families; Chlorophyll a/b binding protein; Structural genes; Transcription; Gene expression; Genetic regulation; Messenger RNA; Embryogenesis; Plant development; Stems; Roots; Cotyledons; Ribulose-bisphosphate carboxylase

Abstract: The levels of chlorophyll a/b-binding protein (Cab) gene polysomal poly(A)+ mRNA were quantitated throughout the development of Glycine max L. Cab mRNAs were abundant in young expanding leaves, representing 6.1% of the leaf mRNA population. Lower Cab mRNA levels were present in embryos, stems, and cotyledons of developing seedlings; the lowest levels were found in roots where they accounted for 0.04% of the polysomal poly(A)+ mRNA of this organ. To determine the contribution of different members of the Cab gene family to the Cab mRNA populations, a quantitative S1 nuclease reconstruction assay was developed. Cab3, Cab4, and Cab5 mRNAs were detected in all stages examined during soybean development but their levels underwent differential changes. Cab3 encodes the most abundant Cab mRNA in young leaves, developing embryos, and in Stage VII cotyledons from the developing soybean seedling. The levels of Cab mRNAs were compared to the levels of ribulose-1,5-bisphosphate carboxylase small subunit gene mRNA and differences in their patterns of accumulation were noted. Collectively these data indicate that during soybean embryogenesis developmental control mechanisms supersede light-regulatory signals.

35 NAL Call. No.: QK710.P62 Cis-acting regulatory regions of the soybean seed storage 11S globulin gene and their interactions with seed embryo factors. Itoh, Y.; Kitamura, Y.; Arahira, M.; Fukazawa, C. Dordrecht : Kluwer Academic Publishers; 1993 Mar. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 21 (6): p. 973-984; 1993 Mar. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Agrobacterium tumefaciens; Structural genes; Globulins; Seeds; Promoters; Deletions; Recombinant DNA; Reporter genes; Beta-glucuronidase; Gene expression; Genetic regulation; Binding site; Dna binding proteins; Transgenic plants; Genetic transformation; Plant embryos; Embryogenesis

Abstract: A 2.2 kb fragment containing the 5'-flanking region of the soybean glycinin A2B1a gene and its successive deletions with a shorter 5'-flanking sequence were fused, in frame, to the beta-glucuronidase (GUS) reporter gene. The resultant fusions were introduced into tobacco plants via Agrobacterium tumefaciens. Assays of the GUS activity in seeds of transgenic tobacco showed that the upstream region, -657 to -327 (relative to the transcription initiation site [ + 1 ]), of the glycinin gene is required for optimal expression of the transformed gene. Interactions between embryo nuclear factors and DNA fragments covering the downstream region of -326, in which are included the TATA box and legumin boxes, were not apparent. The embryo factors capable of binding specifically to three subregions, -653 to -527, -526 to -422, and -427 to -321, of the upstream regulatory region were detected. Such factors appeared to be organ-specific and could be found solely in developing seeds at the early middle stage of embryogenesis (around 24 days after flowering). Evidence obtained by characterizing the nature of the binding proteins and by gel mobility shift assays established that the same factor does interact with a consensus motif 5'-ATA/TATTTCN-/CTA-3' which occurs four times in the cis-acting regulatory region between -657 and -327. Moreover, this conserved motif could also be found in the 5' regulatory region of another glycinin A1aB1b gene. Thus it is likely that the observed interaction between the nuclear factor and the conserved motifs would lead to activation of transcription from the glycinin genes in maturing soybean seeds.

36 NAL Call. No.: QK710.P68 Cis-analysis of a seed protein gene promoter: the conservative RY repeat CATGCATG within the legumin box is essential for tissue-specific expression of a legumin gene.
Baumlein, H.; Nagy, I.; Villarroel, R.; Inze, D.; Wobus, U. Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992 Mar.
The plant journal v. 2 (2): p. 233-239; 1992 Mar. Includes references.

Language: English

Descriptors: Vicia faba; Nicotiana tabacum; Seeds; Protein synthesis; Genetic regulation; Promoters; Gene expression; Legumin; Dna; Nucleotide sequences

37 NAL Call. No.: QK710.P62 Cloning and expression of an embryo-specific mRNA up-regulated in hydrated dormant seeds.
Goldmark, P.J.; Curry, J.; Morris, C.F.; Walker-Simmons, M.K. Dordrecht : Kluwer Academic Publishers; 1992 Jun. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (3): p. 433-441; 1992 Jun. Includes references.

Language: English

Descriptors: Bromus secalinus; Gene expression; Genetic regulation; Messenger RNA; Cloning; Nucleotide sequences; Amino acid sequences; Plant embryos; Seeds; Seed dormancy; Imbibition; Abscisic acid

Abstract: Dormant seeds do not germinate when imbibed in water even when conditions are favorable for germination. These hydrated seeds remain viable, but growth-arrested for weeks due to unknown restrictions within the embryo. As a model system for the study of the molecular processes occurring in dormant seeds, we have chosen to examine gene expression in Bromus secalinas, a grass species that produces seeds with high levels of embryonic dormancy. Using differential screening for mRNAs present in hydrated dormant embryos, we have identified a cDNA clone, pBS128, that encodes a mRNA transcript found in the embryos of hydrated seeds of B. secalinus as well as in embryos from mature dry seeds. Striking differences in pBS128 transcript levels appear upon hydration of dormant and nondormant seeds. Upon imbibition pBS128 transcript levels increase over four-fold in dormant seeds, but rapidly decline and disappear in nondormant seeds, which subsequently germinate. The pBS128 transcript appears to be embryo-specific since the transcript is not detectable in either non-stressed or dehydrated seedling tissue. Application of 50 micromolar ABA to nondormant seeds arrests germination and enhances pBS128 transcript levels. The nucleotide sequence of the nearly full-length pBS128 cDNA shows no homology to other reported genes, and the putative protein sequence does not exhibit the hydrophilic characteristics of the ABA-responsive LEA (late embryogenesis abundant) proteins.

38 NAL Call. No.: 448.3 Ar23 The coat protein genes of squash mosaic virus: cloning, sequence analysis, and expression in tobacco protoplasts.
Hu, J.S.; Pang, S.Z.; Nagpala, P.G.; Siemieniak, D.R.; Slightom, J.L.; Gonsalves, D.
Wien : Springer,; 1993.
Archives of virology v. 130 (1/2): p. 17-31; 1993. Includes references.

Language: English

Descriptors: Squash mosaic comovirus; Coat proteins; Genes; Cloning; Amino acid sequences; Nucleotide sequences; Dna sequencing; Gene expression; Tobacco; Protoplasts; In vitro

Abstract: Complementary DNA of the middle-component RNA of the melon strain of squash mosaic comovirus (SqMV) was cloned. Clones containing the coat protein genes were identified by hybridization with a degenerate oligonucleotide synthesized according to the amino acid sequence of a purified peptide fragment of the SqMV large coat protein. A clone containing of 2.5 kbp cDNA insert of SqMV M-RNA was sequenced. The total insert sequence of 25 10 bp included a 2373 bp open reading frame (ORF) (encoding 791 amino acids), a 123 bp 3'-untranslated region, and a poly(A) region. This ORF is capable of encoding both the 42 and 22 k SqMV coat proteins. Direct N-terminal sequence analysis of the 22 k coat protein revealed its presence at the 3' end of this ORF and the position of the proteolytic cleavage site (Q/S) used to separate the large and small coat proteins from each other. A putative location of the N-terminal proteolytic cleavage site of the 42 k coat protein (Q/N) was predicted by comparisons with the corresponding coat proteins of cowpea mosaic virus, red clover mottle virus, and bean-pod mottle virus. Although the available nucleotide sequences of these viruses revealed little similarity, their encoded coat proteins shared about 47% identity. The identity of the encoded 42 k and 22 k peptides was confirmed by engineering the respective regions for expression followed by transfer into tobacco protoplasts using the polyethylene glycol method. Both SqMV coat proteins were expressed in vivo as determined by their reactivity to SqMV coat protein specific antibodies.

39 NAL Call. No.: 450 P692 Cold-induced changes in freezing tolerance, protein phosphorylation, and gene expression: evidence for a role of calcium. Monroy, A.F.; Sarhan, F.; Dhindsa, R.S. Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug. Plant physiology v. 102 (4): p. 1227-1235; 1993 Aug. Includes references.

Language: English

Descriptors: Medicago sativa; Freezing; Tolerance; Plant proteins; Phosphorylation; Regulation; Calcium ions; Cell suspensions; Phosphoproteins; Gene expression; Messenger RNA; Cold; Acclimatization; Metabolic inhibitors; Enzyme inhibitors; Protein kinase

Abstract: The role of Ca2+ in cold-induced changes in protein phosphorylation, gene expression, and development of freezing tolerance has been studied in cell-suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago sativa spp. falcata cv Anik). Chemical treatments to block Ca2+ channels, antagonize calmodulin action, or inhibit protein kinases markedly inhibited the cellular capacity to develop cold-induced freezing tolerance but had little effect on cell viability. An analysis of phosphoprotein profile by two-dimensional polyacrylamide gel electrophoresis revealed that at low temperature the relative level of phosphorylation of several proteins increased, whereas that of several others decreased. When cold acclimation was carried out in the presence of N-(6-amino-hexyl)-5-chloro-1-naphthalene-sulfonamide hydrochloride, an antagonist of calmodulin and Ca2+-dependent protein kinases, or the Ca2+ channel blocker La3+, the cold-induced changes in protein phosphorylation were strongly inhibited, cells lost their capacity to develop freezing tolerance, and accumulation of transcripts of cold acclimation-specific genes was substantially reduced. An inhibitor of protein kinases, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had less pronounced effects on the cold-induced protein phosphorylation and caused only a partial inhibition of the cold-induced development of freezing tolerance and accumulation of the transcripts. The level of phosphorylation of one protein, of about 15 kD, increased more than 10-fold at low temperature and showed a strong positive correlation with cold-induced freezing tolerance and gene expression even when the latter were altered with various chemical treatments. These results suggest that Ca and protein phosphorylation, or perhaps a coupling of the two, play an important role during the acquisition of freezing tolerance during cold acclimation.

40 NAL Call. No.: 500 N21P Combination of H-box [CCTACC(N)7CT] and G-box (CACGTG) cis elements is necessary for feed-forward stimulation of a chalcone synthase promoter by the phenylpropanoid-pathway intermediate p-coumaric acid. Loake, G.J.; Faktor, O.; Lamb, C.J.; Dixon, R.A. Washington, D.C. : The Academy; 1992 Oct01. Proceedings of the National Academy of Sciences of the United States of America v. 89 (19): p. 9230-9234; 1992 Oct01. Includes references.

Language: English

Descriptors: Medicago sativa; Phaseolus vulgaris; Gene expression; Genetic regulation; Growth promoters; Naringenin-chalcone synthase; Nucleotide sequences; P-coumaric acid

Abstract: The phenylpropanoid pathway intermediate p-coumaric acid (4-CA) stimulated expression of the bean (Phaseolus vulgaris L.) chalcone synthase (malonyl-CoA:4-coumaroyl-CoA, EC 2.3.1.74) chs15 gene promoter in electroporated protoplasts of alfalfa (Medicago sativa L.). We have analyzed the effects of 5' deletions, mutations, and competition with promoter sequences in trans on the expression of a chs15 promoter-chloramphenicol acetyltransferase gene fusion in elicited alfalfa protoplasts. Two distinct sequence elements, the H-box (consensus CCTACC(N)7CT) and the G-box (CACGTG), are required for stimulation of the chs15 promoter by 4-CA. Furthermore, a 38-base-pair chs15 promoter sequence containing both cis elements conferred responsiveness to 4-CA on the cauliflower mosaic virus 35S minimal promoter. The H-box and G-box in combination establish the complex developmental pattern of chs15 expression and are also involved in stress induction. Hence, potential internal pathway regulation through feed-forward stimulation by 4-CA operates by modulation of the signal pathways for developmental and environmental regulation.

41 NAL Call. No.: QK710.P62 A complex ensemble of cis-regulatory elements controls the expression of a Vicia faba non-storage seed protein gene. Fiedler, U.; Filistein, R.; Wobus, U.; Baumlein, H. Dordrecht : Kluwer Academic Publishers; 1993 Jul. Plant molecular biology v. 22 (4): p. 669-679; 1993 Jul. Includes references.

Language: English

Descriptors: Vicia faba; Structural genes; Plant proteins; Seeds; Promoters; Deletions; Gene expression; Transcription; Genetic regulation; Genetic transformation; Transgenic plants; Reporter genes; Beta-glucuronidase; Histoenzymology; Nicotiana tabacum

Abstract: We have identified cis-regulatory elements within the 5'-upstream region of a Vicia faba non-storage seed protein gene, called usp, by studying the expression of usp-promoter deletion fragments fused to reporter genes in transgenic tobacco seeds. 0.4 kb of usp upstream sequence contain at least six, but probably more, distinct cis-regulatory elements which are responsible for seemingly all quantitative, spatial and temporal aspects of expression. Expression-increasing and -decreasing elements are interspersed and include an AT-rich sequence, a G-box element and a CATGCATG motif. The latter acts as a negative element in contrast to what has been found for the same motif in legumin- and vicilin-type seed storage protein gene promoters. Seed specificity of expression is mainly determined by the -68/+51 region which confers, however, only very low levels of expression. The data support the combinatorial model of promoter function.

42 NAL Call. No.: QH426.C8 Complex organization of the soybean mitochondrial genome: recombination repeats and multiple transcripts at the atpA loci. Chanut, F.A.; Grabau, E.A.; Gesteland, R.F. Berlin ; New York : Springer-Verlag, 1979-; 1993. Current genetics v. 23 (3): p. 234-247; 1993. Includes references.

Language: English

Descriptors: Glycine max; Loci; Structural genes; Plant proteins; Mitochondrial DNA; Repetitive DNA; Nucleotide sequences; Amino acid sequences; Pseudogenes; Restriction mapping; Mitochondrial genetics; Transcription; Gene expression; Messenger RNA; Multiple genes; Homologous recombination

Abstract: Identification of the soybean mitochondrial atpA open reading frame (atpA ORF) was based on sequence similarity with atpA genes in other plant mitochondria and partial protein sequencing. The atpA reading frame ends with four tandem UGA codons which overlap four tandem AUG codons initiating an unidentified reading frame, orf214. The atpA-orf214 region is found in multiple sequence contexts in soybean mitochondrial DNA (mtDNA), which can be attributed to the presence of two recombination repeats. A 1-kb repeat spans 600 nucleotides (nt) of atpa N-terminal coding region and 400 nt of upstream sequence. Its four configurations correspond to two full-length atpA-orf214 genes and two truncated pseudogenes. A 2-kb repeat lies 3 kb downstream from the 1-kb repeat. Restriction maps of cosmid clones suggest that a 10-kb segment containing both repeats is itself duplicated in the mt genome. With two recombination repeats present in a total of three copies per genome, soybean mtDNA is expected to consist of a complex population of subgenomic molecules. Transcription of the atpa loci was analysed by Northern blotting and S1 nuclease protection. The atpA genes express multiple transcripts with one major 3' end and heterogeneous 5' sequences extending several kb upstream of the atpA coding region. The atpa gene and orf214 are co-transcribed on all major transcripts. The pseudogenes do not express stable RNAs.

43 NAL Call. No.: 381 B523 Conserved histidine residues in soybean lipoxgenase: functional consequences of their replacement.
Steczko, J.; Donoho, G.P.; Clemens, J.C.; Dixon, J.E.; Axelrod, B. Washington, D.C. : American Chemical Society; 1992 Apr28. Biochemistry v. 31 (16): p. 4053-4057; 1992 Apr28. Includes references.

Language: English

Descriptors: Glycine max; Lipoxygenase; Histidine; Amino acid sequences; Mutations; Gene expression; Cloning; Enzyme activity; Binding site

Abstract: Sequences of 13 lipoxygenases from various plant and mammalian species, thus far reported, display a motif of 38 amino acid residues which includes 5 conserved histidines and a 6th histidine about 160 residues downstream. These residues occur at positions 494, 499, 504, 522, 531, and 690 in soybean lipoxygenase isozyme L-1. Since the participation of iron in the lipoxygenase reaction has been established and existing evidence based on Mossbauer and EXAFS spectroscopy suggests that histidines may be involved in iron binding, the effect of the above residues has been examined in soybean lipoxygenase L-1. Six singly mutated lipoxygenases have been produced in which each of the His residues has been replaced with glutamine. Two additional mutants have been constructed wherein the codons for His-494 and His-504 have been replaced by serine codons. All of the mutant lipoxygenases, which were obtained by expression in Escherichia coli, have mobilities identical to that of the wild-type enzyme on denaturing gel electrophoresis and respond to lipoxygenase antibodies. The mutated proteins H499Q, H504Q, H504S, and H690Q are virtually inactive, while H522Q has about 1% of the wild-type activity. H494Q, H494S, and H531Q are about 37%, 8%, and 20% as active as the wild type, respectively. His-517 is conserved in the several lipoxygenase isozymes but not in the animal isozymes. The mutant H517Q has about 33% of the wild-type activity. The inactive mutants, H499Q, H504Q, H504S, and H690Q, become insoluble when heated for 3 min at 65 degrees C, as does H522Q. The other mutants and the wild-type are stable under these conditions. Although the essentiality of His-499, -504, and -690 is not proven, they are tentatively considered to be prime candidates for iron ligands. Judgment on the role of H-522 is more uncertain, since mutant H522Q has weak but detectable activity. The Km values of the active mutants and the wild-type L-1, when determined against linoleic acid, differ only moder

44 NAL Call. No.: 450 P692 Constitutive and inducible aerobic and anaerobic stress proteins in the Echinochloa complex and rice.
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.

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.

45 NAL Call. No.: QK710.P62 Constitutive expression of the beta-phaseolin gene in different tissues of transgenic alfalfa does not ensure phaseolin accumulation in non-seed tissue. Bagga, S.; Sutton, D.; Kemp, J.D.; Sengupta-Gopalan, C. Dordrecht : Kluwer Academic Publishers; 1992 Sep. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (6): p. 951-958; 1992 Sep. Includes references.

Language: English

Descriptors: Phaseolus vulgaris; Medicago sativa; Agrobacterium tumefaciens; Structural genes; Multigene families; Introns; Exons; Phaseolin; Recombinant DNA; Cauliflower mosaic caulimovirus; Promoters; Genetic transformation; Transgenics; Gene expression; Seeds; Roots; Root nodules; Leaves; Stems; Reporter genes; Phosphotransferases; Ligases

Abstract: Phaseolin is a glycoprotein that constitutes the major storage protein in bean seeds. The phaseolin gene promoters function in a seed-specific manner. In an attempt to understand if events following transcription of the gene also contribute to the seed-specific accumulation of the phaseolin protein, we studied the effect of substituting the constitutive CaMV-35S promoter for the beta-phaseolin gene promoter on expression of the phaseolin gene in different plant organs. A chimeric gene consisting of the 35S promoter, the coding sequence of the beta-phaseolin gene (all five introns and six exons) and the 3'-flanking region of the beta-phaseolin gene, was introduced into alfalfa via Agrobacterium tumefaciens. While all organs examined shared high levels of phaseolin transcripts, the only organ that showed significant accumulation of the phaseolin protein were the mature seeds. Co-migration of the major immunoreactive polypeptides from the non-seed organs with the authentic beta-phaseolin polypeptides on SDS-PAGE indicates that the protein in non-seed organs undergoes correct post-translational processing and modification, but are more unstable in a non-seed environment.

46 NAL Call. No.: 450 P692 Contrasting storage protein synthesis and messenger RNA accumulation during development of zygotic and somatic embryos of alfalfa (Medicago sativa L.). Krochko, J.E.; Pramanik, S.K.; Bewley, J.D. Rockville, Md. : American Society of Plant Physiologists; 1992 May. Plant physiology v. 99 (1): p. 46-53; 1992 May. Includes references.

Language: English

Descriptors: Medicago sativa; Plant embryos; Somatic embryogenesis; Zygotes; Plant proteins; Protein synthesis; Genetic regulation; Messenger RNA; Gene expression; Seed development

Abstract: During development on hormone-free media, somatic embryos pass through distinct morphological stages that superficially resemble those of zygotic embryo development (globular, heart, torpedo, cotyledonary stages). Despite these similarities, they differ from zygotic embryos in the extent of cotyledonary development and the patterns of synthesis and quantitative expression of seed-specific storage proteins (7S, 11S, and 2S proteins). Alfin (7S) is the first storage protein synthesized in developing zygotic embryos (stage IV). The 11S (medicagin) and 2S (Low Molecular Weight, LMW) storage proteins are not detectable until the following stage of development (stage V), although all three are present before the completion of embryo enlargement. Likewise, the 7S storage protein is the first to be synthesized in developing somatic embryos (day 5). Medicagin is evident by day 7 and the LMW protein by day 10. In contrast to zygotic embryos, alfin remains the predominant storage protein in somatic embryos throughout development. Not only are the relative amounts of medicagin and the LMW protein reduced in somatic embryos but the LMW protein is accumulated much later than the other proteins. Quantification of the storage protein mRNAs (7S, 11 S, and 2S) by northern blot analysis confirms that there are substantial differences in the patterns of message accumulation in zygotic and somatic embryos of alfalfa (Medicago sativa). In zygotic embryos, the 7S, 11S, and 2S storage protein mRNAs are abundant during maturation and, in particular, during the stages of maximum protein synthesis (alfin, stages VI and VII; medicagin, stage VII; LMW, stage VII). In somatic embryos, the predominance of the 7S storage protein is correlated with increased accumulation of its mRNA, whereas the limited synthesis of the 11S storage protein is associated with much lower steady-state levels of its message. The mRNA for the LMW protein is present already by 3 days after transfer to hormone-free medi

47 NAL Call. No.: 450 P692 Coregulation of soybean vegetative storage protein gene expression by methyl jasmonate and soluble sugars.
Mason, H.S.; DeWald, D.B.; Creelman, R.A.; Mullet, J.E. Rockville, Md. : American Society of Plant Physiologists; 1992 Mar. Plant physiology v. 98 (3): p. 859-867; 1992 Mar. Includes references.

Language: English

Descriptors: Glycine max; Protein synthesis; Gene expression; Regulation; Jasmonic acid; Sucrose; Messenger RNA; Fructose; Glucose; Injuries; Photosynthesis

Abstract: The soybean vegetative storage protein genes vspA and vspB are highly expressed in developing leaves, stems, flowers, and pods as compared with roots, seeds, and mature leaves and stems. In this paper, we report that physiological levels of methyl jasmonate (MeJA) and soluble sugars synergistically stimulate accumulation of vsp mRNAs. Treatment of excised mature soybean (Glycine max Merr. cv Williams) leaves with 0.2 molar sucrose and 10 micromolar MeJA caused a large accumulation of vsp mRNAs, whereas little accumulation occurred when these compounds were supplied separately. In soybean cell suspension cultures, the synergistic effect of sucrose and MeJA on the accumulation of vspB mRNA was maximal at 58 millimolar sucrose and was observed with fructose or glucose substituted for sucrose. In dark-grown soybean seedlings, the highest levels of vsp mRNAs occurred in the hypocotyl hook, which also contained high levels of MeJA and soluble sugars. Lower levels of vsp mRNAs, MeJA, and soluble sugars were found in the cotyledons, roots, and nongrowing regions of the stem. Wounding of mature soybean leaves induced a large accumulation of vsp mRNAs when wounded plants were incubated in the light. Wounded plants kept in the dark or illuminated plants sprayed with dichlorophenyldimethylurea, an inhibitor of photosynthetic electron transport showed a greatly reduced accumulation of vsp mRNAs. The time courses for the accumulation of vsp mRNAs induced by wounding or sucrose/MeJA treatment were similar. These results strongly suggest that vsp expression is coregulated by endogenous levels of MeJA (or jasmonic acid) and soluble carbohydrate during normal vegetative development and in wounded leaves.

48 NAL Call. No.: 442.8 J8224 Crystallization and preliminary X-ray crystallographic analysis of the soybean proglycinin expressed in Escherichia coli. Utsumi, S.; Gidamis, A.B.; Mikami, B.; Kito, M. London ; New York : Academic Press, 1959-; 1993 Sep05. Journal of molecular biology v. 233 (1): p. 177-178; 1993 Sep05. Includes references.

Language: English

Descriptors: Glycine max; Globulins; Seeds; Precursors; X ray diffraction; Molecular conformation; Crystals; Crystallization; Recombinant DNA; Gene expression; Escherichia coli

Abstract: Glycinin is one of the dominant storage proteins of soybean seeds. Soybean proglycinin expressed in Escherichia coli has been crystallized from Tris.HCl buffer (pH 7.6) by the dialysis equilibrium method. The crystals belong to the tetragonal system, Space group P41 or P43, with unit cell dimensions of a=b=115.2 A, and c=147.1 A. The asymmetric unit contains three molecules of proglycinin, with crystal volume per protein mass (Vm) of 3.05 A(3)/Da and solvent content of 58.4% by volume. The crystals diffract X-rays to a resolution limit of at least 2.9 A and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.

49 NAL Call. No.: QK725.P56 1993 Cytoplasmic male sterility in sunflower. Smart, C.J.; Moneger, F.; Leaver, C.J.
Weinheim ; New York : VCH; 1993.
Plant mitochondria : with emphasis on RNA editing and cytoplasmic male sterility /. p. 403-410; 1993. Includes references.

Language: English

Descriptors: Helianthus annuus; Mitochondrial DNA; Cytoplasmic male sterility; Mitochondrial genetics; Molecular mapping; Restriction mapping; Transcription; Gene expression

50 NAL Call. No.: QK710.P62 Cytoplasmic ribosomal protein S15a from Brassica napus: molecular cloning and developmental expression in mitotically active tissues. Bonham-Smith, P.C.; Oancia, T.L.; Moloney, M.M. Dordrecht : Kluwer Academic Publishers; 1992 Mar. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (5): p. 909-919; 1992 Mar. Includes references.

Language: English

Descriptors: Brassica napus; Multigene families; Ribosomes; Proteins; Cloning; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Leaves; Flowers; Buds; Apical meristems

Abstract: We have isolated two cDNA clones which appear to encode the 40S ribosomal subunit protein S15a from Brassica napus (oilseed rape). The open reading frame in both clones contains 390 bases, encoding a deduced polypeptide sequence of 130 amino acids (100% homology between clones) with 76% sequence identity to the N-terminal 37 amino acids of the rat ribosomal protein S15a and 80% identity to the S24 polypeptide of yeast. Both the yeast and rapeseed proteins have a net positive charge of + 9 and the rapeseed S15a protein has a molecular mass of 14,778 Da compared to 14,762 Da for the yeast protein. The rapeseed ribosomal protein S15a is encoded by a small multi-gene family with at least two actively transcribed members. A single transcript of ca. 1.0 kb, corresponding to ribosomal protein S15a, is abundant in actively dividing tissues such as apical meristem, flower buds and young leaves and less abundant in mature stem and fully expanded leaves.

51 NAL Call. No.: QK710.P62 Deletion analysis and localization of SbPRP1, a soybean cell wall protein gene, in roots of transgenic tobacco and cowpea. Suzuki, H.; Fowler, T.J.; Tierney, M.L. Dordrecht : Kluwer Academic Publishers; 1993 Jan. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 21 (1): p. 109-119; 1993 Jan. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Vigna aconitifolia; Multigene families; Structural genes; Promoters; Plant proteins; Cell wall components; Genetic transformation; Agrobacterium tumefaciens; Transgenics; Reporter genes; Beta-glucuronidase; Gene expression; Deletions; Histoenzymology; Roots; Epidermis; Agrobacterium rhizogenes; Messenger RNA; Genetic regulation

Abstract: SbPRP1 is a member of the soybean (Glycine max L. Merr) proline-rich cell wall protein family and is expressed at high levels in root tissue. To characterize the sequences required for this expression, we have fused 1.1 kb of upstream flanking DNA sequence from an SbBPRP1 genomic clone to a gene encoding beta-glucuronidase (GUS). This construct was introduced into tobacco using Agrobacterium tumefaciens-mediated transformation. Histochemical staining of GUS activity in transgenic tobacco indicated that SbPRP1 is expressed in the apical and elongating region of both primary and lateral roots, most strongly in the epidermis. A similar localization pattern was found in transformed hairy roots when this construct was introduced into cowpea (Vigna aconitifolia) using Agrobacterium rhizogenes-mediated transformation. Nested 5'-deletion analysis of the SbPRP1 promoter indicated that a minimal promoter for SbPRP1 expression in roots is located within the first 262 bases of upstream flanking DNA and that the region between -1080 and -262 is required for maximal expression of this gene. Gel retardation assays showed that nuclear factors can be detected in soybean roots which specifically bind to sequences located between -1080 and -623, a region which is needed for maximal expression of the SbPRP1 promoter. Northern hybridization analysis was also used to show that little SbPRP1 mRNA was present in roots during the first 24 h after imbibition. These studies indicate that SbPRP1 expression is localized to the actively growing region of the root and that this expression is temporally regulated during very early stages of seedling growth.

52 NAL Call. No.: QK710.P62 Developmental and environmental concurrent expression of sunflower dry-seed-stored low-molecular-weight heat-shock protein and Lea mRNAs. Almoguera, C.; Jordano, J.
Dordrecht : Kluwer Academic Publishers; 1992 Aug. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (5): p. 781-792; 1992 Aug. Includes references.

Language: English

Descriptors: Helianthus annuus; Dna; Structural genes; Heat shock proteins; Plant proteins; Seeds; Plant embryos; Nucleotide sequences; Gene expression; Messenger RNA; Seedlings; Embryogenesis; Genetic regulation; Abscisic acid; Osmotic pressure; Stress; Heat shock

Abstract: We have cloned and sequenced three different cDNAs from sunflower seed-stored mRNA. Sequence similarities and response to heat-shock identified one of the cDNAs a low-molecular-weight heat-shock protein (lmw-HSP). The other two clones showed significant sequence similarity to the cotton and carrot late-embryogenesis-abundant (Lea) proteins D-113 and Emb-1, respectively. The three cDNAs showed similar expression patterns during zygotic embryo development, as well as in vegetative tissues of 3-day-old seedlings in response to stress. Maximal accumulation of all three mRNAs was detected in dry seeds and during embryo mid-maturation stage, in the absence of exogenous stress. In seedlings, mRNAs accumulated to lower levels in response to osmotic stress and exogenous abscisic acid (ABA) treatments. A differential time course of response to osmotic stress was observed: lmw-HSP mRNA accumulation was induced earlier than that of Lea mRNAs. The coordinate accumulation of Lea and lmw-HSP transcripts during embryo development and in response to stress and ABA suggests the existence of common regulatory elements for Lea and lmw-HSP genes, and supports the notion that HSPs might have alternative functions in the plant cell.

53 NAL Call. No.: QK710.P62 Differential expression of a chimeric CaMV-tomato proteinase Inhibitor I gene in leaves of transformed nightshade, tobacco and alfalfa plants. Narvaez-Vasquez, J.; Orozco-Cardenas, M.L.; Ryan, C.A. Dordrecht : Kluwer Academic Publishers; 1992 Dec. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 20 (6): p. 1149-1157; 1992 Dec. Includes references.

Language: English

Descriptors: Lycopersicon esculentum; Solanum nigrum; Nicotiana tabacum; Medicago sativa; Transgenics; Genetic transformation; Structural genes; Proteinase inhibitors; Gene transfer; Gene expression; Recombinant DNA; Promoters; Cauliflower mosaic caulimovirus; Messenger RNA; Leaves; Flowers; Vacuoles; Immunoblotting

Abstract: The open reading frame and terminator region of a wound-inducible tomato Inhibitor I gene, regulated by the CaMV 35S promoter, was stably integrated into the genomes of nightshade (Solanum nigrum), tobacco (Nicotiana tabacum), and alfalfa (Medicago sativa), using an Agrobacterium-mediated transformation system. The expression of the foreign Inhibitor I gene in leaves of each species was studied at the mRNA and protein levels. The levels of Inhibitor I protein present in leaves of each species correlated with the levels of mRNA. The average levels of both mRNA and Inhibitor I protein were highest in leaves of transgenic nightshade plants (over 125 micrograms of Inhibitor I per g tissue), less in tobacco plants (about 75 micrograms/g tissue), and lowest in leaves of transgenic alfalfa plants (below 20 micrograms/g tissue). Inhibitor I protein was observed in all tissues throughout transgenic plant species, but inhibitor concentration per gram of tissue was 2-3 times higher in young developing leaf tissues and floral organs. The differences in the expression of the CaMV-tomato Inhibitor I gene among the different plant genera suggests that either the rate of transcription of the foreign gene or the rate of degradation of the nascent Inhibitor I mRNA varies among genera. Using electron microscopy techniques, the newly synthesized pre-pro-Inhibitor I protein was shown to be correctly processed and stored as a mature Inhibitor I protein within the central vacuoles of leaves of transgenic nightshade and alfalfa. The results of these experiments suggest that maximal expression of foreign proteinase inhibitor genes, and perhaps other foreign defense genes, may require gene constructs that are fashioned with promoters and terminators that allow maximum expression in the selected plant species.

54 NAL Call. No.: QK710.P62 Differential expression of bean chitinase genes by virus infection, chemical treatment and UV irradiation.
Margis-Pinheiro, M.; Martin, C.; Didierjean, L.; Burkard, G. Dordrecht : Kluwer Academic Publishers; 1993 Jul. Plant molecular biology v. 22 (4): p. 659-668; 1993 Jul. Includes references.

Language: English

Descriptors: Phaseolus vulgaris; Structural genes; Chitinase; Gene expression; Messenger RNA; Leaves; Defense mechanisms; Genetic regulation; Alfalfa mosaic virus; Infections; Ultraviolet radiation; Mercuric chloride; Complementary DNA; Nucleotide sequences; Amino acid sequences; Cloning

Abstract: Three chitinases have been shown previously to be induced upon various stresses of bean leaves. Time course studies of mRNA accumulation of two of them (P3- and P4-chitinases) have been studied upon virus infection, mercuric chloride treatment and UV irradiation. In alfalfa mosaic virus (AlMV)-infected plants both mRNAs, absent in uninfected bean leaves, become detectable 36 h after inoculation. A maximum level of mRNAs is reached 84 h after inoculation and, whereas the amount of P3-ch mRNA decreases soon after having reached the maximum, the amount of P4-ch mRNA remains at high levels for several days. In mercuric chloride-treated leaves P4-ch mRNA becomes detectable 1-1.5 h after onset of treatment and a maximum level is observed between 6 h and 24 h after treatment; P3-ch mRNA becomes detectable later than P4-ch mRNA in treated leaves and reaches a maximum as late as 18 h after treatment has been applied. UV light also induces the synthesis of both mRNAs but, here again, important differences are observed in the accumulation rate of the two transcripts. The relative amounts of each mRNA induced by the different stresses have been compared. The most effective inducer of P3-ch mRNA is AlMV. In contrast, mercuric chloride induces P4-ch mRNA more efficiently than AlMV or UV light. We have also determined the complete nucleotide sequence of the cDNA encoding P3-chitinase that has been isolated from a cDNA library by using the cucumber lysozyme-chitinase cDNA as a probe. The 1072 bp P3-ch cDNA encodes a mature protein of 268 amino acid residues and the 25 residue NH2-terminal signal peptide of the precursor. Because of its high structural homology to the cucumber and Arabidopsis acidic chitinases as well as to the N-terminal amino acid sequence of the bifunctional lysozyme-chitinase from P. quinquifolia, bean P3-chitinase can be considered to belong to the class III chitinases. Southern blot analysis of bean genomic DNA revealed that P3-chitinase is encoded by a single gene.

55 NAL Call. No.: 450 P692 Differential expression of histone H3 gene variants during cell cycle and somatic embryogenesis in alfalfa.
Kapros, T.; Bogre, L.; Nemeth, K.; Bako, L.; Gyorgyey, J.; Wu, S.C.; Dudits, D.
Rockville, Md. : American Society of Plant Physiologists; 1992 Feb. Plant physiology v. 98 (2): p. 621-625; 1992 Feb. Includes references.

Language: English

Descriptors: Medicago sativa; Clones; Messenger RNA; Gene expression; Histones; Genetic regulation; Somatic embryogenesis; Cell growth; Transcription

Abstract: Northern analysis has revealed substantial differences in mRNA accumulation of the two histone H3 gene variants represented by ph3c-1 and ph3c-11 cDNA clones. Both in partially synchronized cell suspension cultures and in protoplast-derived cells from alfalfa, Medicago varia, the maximal level of the histone H3-1 gene transcript coincided with the peak in [(3)H]thymidine incorporation. Histone H3-11 mRNA was detectable in cells throughout the period of the cell cycle studied. Various stress factors such as medium replacement, enzyme digestion of the cell wall, osmotic shock, and auxin treatment considerably increased the level of the histone H3-11 transcript. In alfalfa (Medicago sativa), the presence of H3-11 mRNA in unorganized tissues of microcallus suspension and in somatic embryos induced by auxin treatment supports the idea that this H3 variant exists in a continuously active state of transcription. During embryo development, the early globular stage embryos showed increased accumulation of histone H3-11 mRNA in comparison with the later stages. The highest level of the histone H3-1 transcript was detectable 1 day after treatment of callus tissues with 2,4-dichlorophenoxyacetic acid. Somatic embryos contained appreciable levels of histone H3-1 transcripts at all stages of somatic embryo development. These observations suggest that the histone H3-1 gene belongs to the class of replication-dependent histone genes. The histone H3-11 gene showed characteristics of a constitutively expressed replacement-type histone gene, with a specific characteristic that external factors can influence the level of gene transcription.

56 NAL Call. No.: QK725.P54 Differential expression of two peanut peroxidase cDNA clones in peanut plants and cells in suspension culture in response to stress. Breda, C.; Buffard, D.; Huystee, R.B. van; Esnault, R. Berlin, W. Ger. : Springer International; 1993. Plant cell reports v. 12 (5): p. 268-272; 1993. Includes references.

Language: English

Descriptors: Arachis hypogaea; Leaves; Stems; Roots; Cell suspensions; Stress response; Injuries; Ethylene; Gene expression; Peroxidase; Enzyme activity; Transcription; Genes

Abstract: Peanut (Arachis hypogea L.) peroxidase gene expression was analyzed by measuring the accumulation of transcripts in cultured cells and various plant parts (leaf, stem, root) and upon their treatment with ethylene or wounding, respectively. Two transcripts (prxPNC1 and prxPNC2) corresponding to two peroxidase genes are expressed at higher levels in cultured cells as compared to various plant organs. Analysis of total poly(A)+ RNA with an oligonucleotide probe corresponding to a highly conserved region of peroxidase genes showed the expression of three peroxidase related sequences (1,000, 1,400 or 2,600 bp) in stem or leaf but barely detectable in roots. The prxPNC2 transcript transiently expressed at high levels in response to ethylene treatment of cells or wounding of leaves. This suggests that the corresponding gene(s) are expressed in response to stress.

57 NAL Call. No.: 450 P692 Differential expression of two soybean (Glycine max L.) proline-rich protein genes after wounding.
Suzuki, H.; Wagner, T.; Tierney, M.L.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Apr. Plant physiology v. 101 (4): p. 1283-1287; 1993 Apr. Includes references.

Language: English

Descriptors: Glycine max; Structural genes; Plant proteins; Proline; Cell wall components; Gene expression; Messenger RNA; Abiotic injuries; Seedlings; Leaves; Multigene families; Hypocotyls; Roots; Iaa; Naa; 2,4-d

Abstract: We have investigated the wound-induced expression of two members of the soybean (Glycine max L.) proline-rich cell wall protein gene family and show that SbPRP1 and SbPRP2 exhibit unique patterns of expression after physical damage. SbPRP1 mRNA can be detected in the hook of soybean seedlings within 2 h after wounding and is present at high levels in the hook and elongating hypocotyl 20 h after wounding. In contrast, SbPRP2 mRNA increases transiently and rapidly throughout the soybean seedling after wounding. SbPRP2 is also induced by wounding in soybean leaves, but the pattern of mRNA accumulation in leaves is distinct from that seen in seedlings and reaches high levels of expression 20 h after physical damage. SbPRP2 mRNA levels were also found to increase in the mature hypocotyl and roots of seedlings in response to treatment with 10 micromolar indoleacetic acid and naphthalene-1-acetic acid. These data indicate that the wound-induced expression of PRPs in soybean is tissue specific and that the regulation of these genes after physical damage may operate through different signal transduction pathways.

58 NAL Call. No.: 450 P692 Differential expression within the glutamine synthetase gene family of the model legume Medicago truncatula.
Stanford, A.C.; Larsen, K.; Barker, D.G.; Cullimore, J.V. Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Sep. Plant physiology v. 103 (1): p. 73-81; 1993 Sep. Includes references.

Language: English

Descriptors: Medicago truncatula; Gene expression; Genetic code; Nucleic acids; Plant development

Abstract: The glutamine synthetase (GS) gene family of Medicago truncatula Gaertn. contains three genes related to cytosolic GS (MtGSa, MtGSb, and MtGSc), although one of these (MtGSc) appears not to be expressed. Sequence analysis suggests that the genes are more highly conserved interspecifically rather than intraspecifically: MtGSa and MtGSb are more similar to their homologs in Medicago sativa and Pisum sativum than to each other. Studies in which gene-specific probes are used show that both MtGSa and MtGSb are induced during symbiotic root nodule development, although not coordinately. MtGSa is the most highly expressed GS gene in nodules but is also expressed to lower extents in a variety of other organs. MtGSb shows higher levels of expression in roots and the photosynthetic cotyledons of seedlings than in nodules or other organs. In roots, both genes are expressed in the absence of an exogenous nitrogen source. However the addition of nitrate leads to a short-term, 2- to 3-fold increase in the abundance of both mRNAs, and the addition of ammonium leads to a 2-fold increase in MtGSb mRNA. The nitrogen supply, therefore, influences the expression of the two genes in roots, but it is clearly not the major effector of their expression. In the discussion section, the expression of the GS gene family of the model legume M. truncatula is compared to those of other leguminous plants.

59 NAL Call. No.: QK725.P532 Dissection of the functional architecture of a plant defense gene promoter using a homologous in vitro transcription initiation system. Arias, J.A.; Dixon, R.A.; Lamb, C.J.
Rockville, Md. : American Society of Plant Physiologists; 1993 Apr. The Plant cell v. 5 (4): p. 485-496; 1993 Apr. Includes references.

Language: English

Descriptors: Glycine max; Phaseolus vulgaris; Nicotiana tabacum; Promoters; Naringenin-chalcone synthase; Multigene families; Molecular mapping; Transcription; Gene expression; Genetic regulation; In vitro

Abstract: CHS15 is one of a family of bean genes encoding chalcone synthase, which catalyzes the first reaction in a branch pathway of phenylpropanoid biosynthesis for the production of flavonoid pigments and UV protectants and isoflavonoid-derived phytoalexins. The functional architecture of the CHS15 promoter was dissected by a novel homologous plant in vitro transcription initiation system in which whole-cell and nuclear extracts from suspension-cultured soybean cells direct accurate and efficient RNA polymerase II-mediated transcription from an immobilized promoter template. Authentic transcription from the CHS15 promoter template was also observed with whole-cell extracts from suspension-cultured cells of bean, tobacco, and the monocot rice, and the soybean whole-cell extract transcribed several other immobilized promoter templates. Hence, this procedure may be of general use in the study of plant gene regulation mechanisms in vitro. Assay of the effects of depletion of the soybean whole-cell extract by preincubation with small regions of the CHS15 promoter or defined cis elements showed that trans factors that bind to G-box (CACGTG, -74 to -69) and H-box (CCTACC, -61 to -56 and -121 to -126) cis elements, respectively, make major contributions to the transcription of the CHS15 promoter in vitro. Both cis element/trans factor interactions in combination are required for maximal activity. Delineation of these functional cis element/trans factor interactions in vitro provides the basis for study of the mechanisms underlying developmental expression of CHS15 in pigmented petal cells established by G-box and H-box combinatorial interactions, and for characterization of the terminal steps of the signal pathway for stress induction of the phytoalexin defense response.

60 NAL Call. No.: QK725.P532 Downstream DNA sequences are required to activate a gene expressed in the root cortex of embryos and seedlings.
Dietrich, R.A.; Radke, S.E.; Harada, J.J. Rockville, Md. : American Society of Plant Physiologists; 1992 Nov. The Plant cell v. 4 (11): p. 1371-1382; 1992 Nov. Includes references.

Language: English

Descriptors: Brassica napus; Structural genes; Controlling elements; Roots; Cortex; Plant embryos; Seedlings; Genetic regulation; Gene expression; Cell differentiation; Root meristems; Recombinant DNA; Beta-glucuronidase; Reporter genes; Transgenics; Genetic transformation; Embryogenesis

Abstract: We showed previously that a gene, designated AX92, which is expressed at an early stage of cortex differentiation in the root apex of oilseed rape seedlings, is also expressed in embryos. To compare AX92 gene regulation during embryo-genesis and postembryonic growth, we constructed a chimeric gene consisting of AX92 5'and 3' untranslated and flanking regions fused with a beta-glucuronidase protein coding region. We showed that the chimeric gene is active in both developing cortex cells in the root apical meristems of transgenic oilseed rape seedlings and in cortex cells at the root end of embryonic axes. To determine whether the AX92 gene is regulated by a common mechanism in embryos and seedlings, we analyzed the expression of modified chimeric genes. We showed that the AX92 chimeric gene is regulated combinatorially and that DNA sequences located 3' of the protein coding region are necessary for its activation in the root cortex of both embryos and seedlings. Our results suggest that common regulatory sequences are required to activate the gene in the embryonic and postembryonic root cortex.

61 NAL Call. No.: 450 Am36 Duplicate gene expression for isocitrate dehydrogenase and 6-phosphogluconate dehydrogenase in diploid species of Eleusine (Gramineae). Werth, C.R.; Hilu, K.; Langner, C.A.; Baird, W.V. Columbus, Ohio : Botanical Society of America; 1993 Jun. American journal of botany v. 80 (6): p. 705-710; 1993 Jun. Includes references.

Language: English

Descriptors: Eleusine; Plant composition; Isocitrate dehydrogenase; Phosphogluconate dehydrogenase; Isoenzymes; Genetic regulation; Gene expression; Phenotypes; Alleles; Genetic variation; Diploidy; Genetic code; Genetic analysis

Abstract: In the course of a survey of isozyme variation in the grass genus Eleusine, complex band patterns were observed for the enzymes isocitrate dehydrogenase (IDH) and 6-phosphogluconate dehydrogenase (6PGD). These patterns were interpreted as the result of duplicate expression for one of the two genes that ordinarily codes subcellularly compartmentalized forms of each of these enzymes. The interpretation of IDH phenotypes was facilitated by intraspecific allelic variation at one of the putatively duplicated genes (Idh-2), and was verified by examining phenotype ratios in progeny arrays from selfed heterozygotes of E. indica. The lack of analogous intraspecific variation for 6PGD precluded genetic tests, but the duplicate nature of expression was supported by interspecific patterns of variation. Four out of the five diploid species of Eleusine studied (E. indica, E. jaegeri, E. multiflora, E. tristachya) exhibited both duplications; E. floccifolia appeared to lack the IDH duplication, but possessed the 6PGD duplication. Both enzymes showed evidence of hyperduplication in the tetraploid species E. coracana.

62 NAL Call. No.: 450 P692 Effect of brassinolide on gene expression in elongating soybean epicotyls. Clouse, S.D.; Zurek, D.M.; McMorris, T.C.; Baker, M.E. Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov. Plant physiology v. 100 (3): p. 1377-1383; 1992 Nov. Includes references.

Language: English

Descriptors: Glycine max; Gene expression; Genes; Genetic regulation; Brassinolide; 2,4-d; Epicotyls; Length; Seedling growth; Transcription; Messenger RNA

Abstract: We have studied the effect of brassinolide (BR), a plant steroidal lactone, on the expression of auxin-regulated genes in soybean (Glycine max L. cv Williams 82) epicotyls. BR caused up to 4-fold increases in epicotyl length during extended assays at 10-7 M, in the absence of added auxin. Structurally related steroids failed to induce elongation or to alter the BR effect. Northern blot analysis, using sequences corresponding to auxin-regulated genes as probes, has shown that the molecular mechanism of BR-induced elongation is likely to differ from that of auxin-induced elongation in this system. BR does not rapidly induce members of the GH, SAUR, or JCW auxin-inducible gene families before the onset of elongation. BR enhances SAUR and GH1 transcripts after 18 h but has no effect on JCW1 or GH3 transcripts at any time examined. We have shown by two-dimensional gel analysis of in vitro translated mRNA that a submicromolar concentration of BR alters the pattern of gene expression in elongating soybean epicotyls.

63 NAL Call. No.: 381 J8223 Effects of deletion of disulfide bonds by protein engineering on the conformation and functional properties of soybean proglycinin. Utsumi, S.; Gidamis, A.B.; Kanamori, J.; Kang, I.J.; Kito, M. Washington, D.C. : American Chemical Society; 1993 Apr. Journal of agricultural and food chemistry v. 41 (4): p. 687-691; 1993 Apr. Includes references.

Language: English

Descriptors: Glycine max; Targeted mutagenesis; Plant proteins; Precursors; Genetic transformation; Gene transfer; Gene expression; Escherichia coli; Induced mutations; Deletions; Cysteine; Gelation; Gels; Sulfhydryl groups

Abstract: Glycinin, one of the dominant storage proteins of soybean seeds, has two disulfide bonds in subunit: Cys12-Cys45 and Cys88-Cys298 in the proglycinin A(1a)B(1b) subunit. To examine the effects of disrupting disulfide bonds on the formation and maintenance of structure and on the functional properties of proglycinin, we replaced the cysteine residues (Cys12 and Cys88) by oligonucleotide-directed mutagenesis, giving mutant proglycinins Gly12, Ser88 and Gly12Ser88. The mutant proglycinins overproduced in Escherichia coli cells accumulated as soluble proteins and self-assembled into trimers like the native proglycinin. The functional properties of proglycinins Gly12 and Ser88 purified to near homogeneity were examined as models of modified glycinins. Proglycinin Ser88 formed a harder gel than native glycinin and unmodified expressed proglycinin even at the protein concentrations at which native glycinin did not form a hard gel. On the other hand, proglycinin Gly12 formed a gel only at higher protein concentrations (>6%), the hardness of which was similar to that of the native glycinin. Both proglycinins Gly12 and Ser88 exhibited emulsifying activity similar to that of unmodified expressed proglycinin. These results suggest that the number and topology of free sulfhydryl residues are closely related to the heat-induced gel-forming ability and the gel properties of glycinin but not to its emulsification.

64 NAL Call. No.: 450 P692 Effects of sulfur nutrition on expression of the soybean seed storage protein genes in transgenic petunia.
Fujiwara, T.; Hirai, M.Y.; Chino, M.; Komeda, Y.; Naito, S. Rockville, Md. : American Society of Plant Physiologists; 1992 May. Plant physiology v. 99 (1): p. 263-268; 1992 May. Includes references.

Language: English

Descriptors: Petunia; Glycine max; Gene transfer; Transgenics; Gene expression; Seeds; Protein synthesis; Sulfur; Nutrient requirements; Genetic regulation; Methionine

Abstract: The 7S seed storage protein (beta-conglycinin) of soybean (Glycine max [L]. Merr.) has three major subunits; alpha, alpha', and beta. Accumulation of the beta-subunit, but not the alpha- and alpha-subunits, has been shown to be repressed by exogenously applied methionine to the immature cotyledon culture system (LP Holowach, JF Thompson, JT Madison [1984] Plant Physiol 74: 576-583) and to be enhanced under sulfate deficiency in soybean plants (KR Gayler, GE Sykes [1985] Plant Physiol 78: 582-586). Transgenic petunia (Petunia hybrida) harboring either the alpha'- or beta-subunit gene were constructed to test whether the patterns of differential expression were retained in petunia. Petunia regulates these genes in a similar way as soybean in response to sulfur nutritional stimuli, i.e. (a) expression of the beta-subunit gene is repressed by exogenous methionine in in vitro cultured seeds, whereas the alpha'-subunit gene expression is not affected; and (b) accumulation of the beta-subunit is enhanced by sulfur deficiency. The pattern of accumulation of major seed storage protein of petunia was not affected by these treatments. These results indicate that this mechanism of gene regulation in response to sulfur nutrition is conserved in petunia even though it is not used to regulate its own major seed storage proteins.

65 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.
Berlin, W. Ger. : Springer International; 1993. Plant cell reports v. 12 (9): p. 491-495; 1993. Includes references.

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.

66 NAL Call. No.: SB732.6.M65 ENOD8, a novel early nodule-specific gene, is expressed in empty alfalfa nodules.
Dickstein, R.; Prusty, R.; Peng, T.; Ngo, W.; Smith, M.E. St. Paul, MN : APS Press, [c1987-; 1993 Nov. Molecular plant-microbe interactions : MPMI v. 6 (6): p. 715-721; 1993 Nov. Includes references.

Language: English

Descriptors: Medicago sativa; Rhizobium meliloti; Complementary DNA; Structural genes; Nodulins; Nucleotide sequences; Amino acid sequences; Messenger RNA; Gene expression; Root nodules; Nodulation; Mutants

67 NAL Call. No.: 450 P692 Expression and accumulation patterns of nitrogen-responsive lipoxygenase in soybeans.
Grimes, H.D.; Tranbarger, T.J.; Franceschi, V.R. Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Oct. Plant physiology v. 103 (2): p. 457-466; 1993 Oct. Includes references.

Language: English

Descriptors: Glycine max; Lipoxygenase; Enzyme activity; Genetic regulation; Gene expression; Nitrogen; Nutrient availability; Protein synthesis; Messenger RNA; Protein content; Plant composition; Life cycle; Nutrient deficiencies; Amino acids

Abstract: Gene expression and protein accumulation patterns of nitrogen-responsive lipoxygenase (LOX-NR), as a representative vegetative storage protein, were investigated in nonnodulated soybeans (Glycine max [L.] Merr. cv Wye). The form of available nitrogen (supplied as NH4NO3, NH4+, NO3(-1), or urea) influenced the mRNA level and the amount of LOX protein, indicating that preferential accumulation of LOX may occur. Soybeans were grown with 0, 2, 5, and 16 mM total nitrogen to determine the extent to which LOX accumulation responded to soil nitrogen levels. Analysis of both mRNA and protein levels was conducted in shoot tips, stems, pod walls, and leaves over the entire life cycle of the plant. A general correlation between increasing available nitrogen level and LOX level was seen in the shoot tip and other organs throughout the soybean life cycle. However, appreciable amounts of LOX-NR mRNA and protein accumulated even when plants were grown under conditions of nitrogen deficiency. The results indicate that LOX may play an important role as a temporary storage site for amino acids in the developing shoot tip. The expression patterns of LOX-NR in plants grown under nitrogen deficiency suggest that these proteins, although responsive to nitrogen status, may not function solely as temporary storage pools for amino acids.

68 NAL Call. No.: 381 J824 Expression and characterization of the N-terminal doma in of an oleosin protein from sunflower.
Li, M.; Keddie, J.S.; Smith, L.J.; Clark, D.C.; Murphy, D.J. Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993 Aug15.
The Journal of biological chemistry v. 268 (23): p. 17504-17512; 1993 Aug15. Includes references.

Language: English

Descriptors: Helianthus annuus; Plant proteins; Lipid bodies; Molecular conformation; Recombinant DNA; Gene transfer; Gene expression; Escherichia coli

Abstract: Oil bodies of plant seeds contain a triacylglycerol matrix surrounded by a monolayer of phospholipids embedded with alkaline proteins termed oleosins. Although oleosins are amphipathic proteins, they are unlike bilayer membrane proteins since they are associated with a single lipid:water interface at the oil body surface. Oleosins are unusual proteins because they contain a 70-80-residue uninterrupted nonpolar domain, flanked by relative polar C- and N-terminal domains. In the present study, we report the expression of the N-terminal domain of the 18-kDa oleosin isoform from sunflower as a recombinant fusion protein in Escherichia coli and the determination of its secondary structure using CD and Fourier transform infrared spectroscopy either as a purified but partially denatured peptide or reconstituted into liposomes. The structure derived from physical studies was then compared and assigned with those predicted from analysis of the primary sequence of the N-terminal domain. Based on data derived from CD spectroscopy analysis of purified and partially renatured N-terminal polypeptide, it contains about 10% alpha-helical structure, 20-30% beta-strand structure, approximately 8% beta-turn structure, and 60% random coil structure. However, analysis of the polypeptide reconstituted into liposomes showed an increased content of alpha-helical structure to about 20% and an increased beta-strand structure content to about 30-40%. Data derived from Fourier transform infrared spectroscopy studies and compared with the data predicted from the primary sequence showed the peptide is well structured with some antiparallel beta-strand structure from residues 2-9, parallel beta-strand structure from residues 30-37 and/or 42-49, and alpha-helical structure from residues 10-23 and/or 43-49. There is potential amphipathic alpha-helix from residues 10-23. Based on these results, the following model for the secondary structure of the N-terminal domain of sunflower oleosin can be proposed. Residues 2-9 would produce amphipathic antiparallel beta-strand structure. Residues 10-23 would produce an amphipathic alpha-helical structure. Residues 30-37 and/or 42-49 would give parallel beta-strand structure, or residues 42-49 could form a nonpolar alpha-helical structure that would insert into the oil matrix.

69 NAL Call. No.: 381 AR2 Expression cloning in Escherichia coli and preparative isolation of the reductase coacting with chalcone synthase during the key step in the biosynthesis of soybean phytoalexins.
Welle, R.; Schroder, J.
Orlando, Fla. : Academic Press; 1992 Mar. Archives of biochemistry and biophysics v. 293 (2): p. 377-381; 1992 Mar. Includes references.

Language: English

Descriptors: Glycine max; Phytoalexins; Biosynthesis; Naringenin-chalcone synthase; Oxidoreductases; Dna; Cloning; Transformation; Gene expression; Genetic engineering; Purification; Enzyme activity

Abstract: The cDNA for the reductase involved in the biosynthesis of 6'-deoxychalcone (4,2',4'-trihydroxychalcone), the first specific intermediate in the pathway to soybean phytoalexins, was cloned into the expression vector pKK233-2 and transformed into Escherichia coli. Using this source, about 5 mg of homogeneous reductase was isolated from 45 g of cells. The protein purification protocol differs completely from the scheme applied to soybean cell cultures. Size, N-terminal and specific enzyme activities were identical for the plant and E. coli protein. The pure protein is fairly stable, retaining 70% of initial activity after storage at 5 degrees C during 4 weeks. This protein is used for crystallization and in the study of its protein-protein interaction with chalcone synthase.

70 NAL Call. No.: QD415.A1B58 Expression of auxin-responsive genes in soybean and transgenic tobacco. Guilfoyle, T.J.; Hagen, G.; Li, Y.; Gee, M.A.; Ulmasov, T.N.; Martin, G. London : Portland Press; 1992 Feb.
Transactions - Biochemical Society v. 20 (1): p. 97-101; 1992 Feb. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Transgenics; Auxins

71 NAL Call. No.: QK827.S48 Expression of S-locus glycoprotein genes from Brassica oleracea and B. campestris in transgenic plants of self-compatible B. napus cv Westar. Nishio, T.; Toriyama, K.; Sato, T.; Kandasamy, M.K.; Paolillo, D.J.; Nasrallah, J.B.; Nasrallah, M.E.
Heidelberg : Springer International; 1992. Sexual plant reproduction v. 5 (2): p. 101-109; 1992. Includes references.

Language: English

Descriptors: Brassica oleracea; Brassica campestris; Brassica napus; Agrobacterium tumefaciens; Genetic transformation; Transgenics; Gene expression; Self compatibility; Self incompatibility; Glycoproteins; Protein synthesis; Genetic regulation; Immunocytochemistry; Cell ultrastructure; Spatial distribution; Genes

72 NAL Call. No.: 450 P699 Expression of soybean seed storage protein genes in transgenic plants; their effects on expression of a neighboring gene and position dependency. Fujiwara, T.; Beachy, R.N.
Kyoto : Japanese Society of Plant Physiologists; 1993 Jan. Plant and cell physiology v. 34 (1): p. 13-20; 1993 Jan. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Agrobacterium; Genetic transformation; Transgenic plants; Gene expression; Seeds; Plant proteins; Genes; Reporter genes; Beta-glucuronidase; Enzyme activity

Abstract: The beta-conglycinin genes, which encode the 7S seed storage proteins of soybean, were previously shown to be relatively independent of "position effects" in transgenic plants, i.e., expression levels of the (alpha)' and beta subunit genes of beta-conglycinin were relatively consistent on a per gene basis compared with other plant genes. We tested whether the promoter region of the (alpha)' subunit gene confers position independency by introducing a fusion gene comprised of the (alpha)' subunit promoter and the uidA (encoding beta-glucuronidase) coding sequence and found that the resultant gene lost its position independency. We also tested the possibility that the beta-conglycinin genes have the ability to neutralize "position effects" by placing a position dependent gene adjacent to the beta-conglycinin genes. Genes comprised of the promoter that produces the 35S transcript of the cauliflower mosaic virus (CaMV 35S) and the uidA coding region was employed as a position dependent reporter gene. Neither the (alpha)' nor the beta subunit genes effectively altered position dependency of the CaMV 35S promoter. We conclude that the coding sequence of the (alpha)' subunit gene is important for its position independency and that the beta-conglycinin genes do not affect position dependency of the adjacent genes. Nevertheless the (alpha)' subunit gene acts as an enhancer on the CaMV 35S promoter when the promoters are adjacent to each other.

73 NAL Call. No.: 450 P693 Expression of soybean-embryo lipoxygenase 2 in transgenic tobacco tissue. Deng, W.; Grayburn, W.S.; Hamilton-Kemp, T.R.; Collins, G.B.; Hildebrand, D.F. Berlin : Springer-Verlag; 1992.
Planta v. 187 (2): p. 203-208; 1992. Includes references.

Language: English

Descriptors: Nicotiana tabacum; Transgenics; Gene expression; Glycine max; Plant embryos; Lipoxygenase; Enzyme activity; Lipid metabolism; Fatty acids; Peroxidation

Abstract: To assess the role of lipoxygenase (LOX; EC 1.13.11.12) in plants, we increased the expression of LOX in the tissues of Nicotiana tabacum L. cv. 'KY 14' by over-expression of the LOX2 gene from the soybean (Glycine max (L.) Merrill) embryo. The LOX2 cDNA was manipulated by replacing its 5'-untranslated sequence with the translational enhancer of the alfalfa mosaic virus (AMV), and subcloned into a plant expression vector, 3' to a duplicated cauliflower mosaic virus 35S promoter. The AMV-LOX2 construct was transferred into tobacco using Agrobacterium tumefaciens strain A281. The LOX2 was expressed in transgenic tobacco calli, leaves of transgenic plants, and their seed progeny at levels up to 0.1-0.2% of the total extracted protein. The introduced LOX2 affected fatty-acid oxidative metabolism as evidenced by a 50-529% increase in C6-aldehyde production. The impact on C6-aldehyde formation was greater than the effect on production of fatty-acid hydroperoxides. This is consistent with other studies indicating the greater propensity of soybean embryo LOX2 in generating C6-aldehydes than that of other well-characterized LOX isozymes.

74 NAL Call. No.: 450 P692 Expression of the soybean (Glycine max) glutamate 1-semialdehyde aminotransferase gene in symbiotic root nodules. Sangwan, I.; O'Brian, M.R.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul. Plant physiology v. 102(3): p. 829-834; 1993 Jul. Includes references.

Language: English

Descriptors: Glycine max; Structural genes; Complementary DNA; Aminotransferases; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Enzyme activity; Root nodules; Leaves; Etiolation

Abstract: Extracts of soybean (Glycine max) root nodules and greening etiolated leaves catalyzed radiolabeled 6-aminolevulinic acid (ALA) formation from 3,4-[3H]glutamate but not from 1-[14C]glutamate. Nevertheless, those tissue extracts expressed the activity of glutamate 1-semialdehyde (GSA) aminotransferase, the C5 pathway enzyme that catalyzes ALA synthesis from GSA for tetrapyrrole formation. A soybean nodule cDNA clone that conferred ALA prototrophy, GSA aminotransferase activity, and glutamate-dependent ALA formation activity on an Escherichia coli GSA aminotransferase mutant was isolated. The deduced product of the nodule cDNA shared 79% identity with the GSA aminotransferase expressed in barley leaves, providing, along with the complementation data, strong evidence that the cDNA encodes GSA aminotransferase. GSA aminotransferase mRNA and enzyme activity were expressed in nodules but not in uninfected roots, indicating that the Gsa gene is induced in the symbiotic tissue. The Gsa gene was strongly expressed in leaves of etiolated plantlets independently of light treatment and, to a much lesser extent, in leaves of mature plants. We conclude that GSA aminotransferase, and possibly the C5 pathway, is expressed in a nonphotosynthetic plant organ for nodule heme synthesis and that Gsa is a regulated gene in soybean.

75 NAL Call. No.: SB732.6.M65 Extracellular protein elicitors from Phytophthora: host-specificity and induction of resistance to bacterial and fungal phytopathogens. Kamoun, S.; Young, M.; Glascock, C.B.; Tyler, B.M. St. Paul, Minn. : APS Press; 1993 Jan.
Molecular plant-microbe interactions : MPMI v. 6 (1): p. 15-25; 1993 Jan. Includes references.

Language: English

Descriptors: Raphanus sativus; Brassica campestris; Nicotiana tabacum; Crops; Leguminosae; Solanaceae; Phytophthora nicotianae var. parasitica; Phytophthora cryptogea; Xanthomonas campestris pv. armoraciae; Proteins; Cell wall components; Induced resistance; Disease resistance; Genetic regulation; Gene expression; Promoters; Naringenin-chalcone synthase

76 NAL Call. No.: QK710.P62 Ferritin (mRNA, protein) and iron concentrations during soybean nodule development.
Ragland, M.; Theil, E.C.
Dordrecht : Kluwer Academic Publishers; 1993 Feb. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 21 (3): p. 555-560; 1993 Feb. Includes references.

Language: English

Descriptors: Glycine max; Gene expression; Messenger RNA; Ferritin; Iron; Nodulation; Root nodules; Nitrogenase; Enzyme activity; Leghemoglobin

Abstract: To study how iron-rich nodules concentrate and store iron, ferritin (mRNA, protein) was analyzed in developing soybean nodules and compared to nitrogenase (mRNA/activity) and leghemoglobin (mRNA, protein, heme). Both ferritin mRNA and protein concentrations increased early in nodulation. Later in nodulation ferritin protein declined, in contrast to the mRNA, as nitrogenase (mRNA and activity) increased and leghenioglobin (mRNA and protein) accumulated. A precursor/product relationship between iron stored in ferritin and iron in nitrogenase or leghemoglobin is suggested. The uncoordinated changes in ferritin mRNA and protein during nodulation contrast with nitrogenase mRNA and nitrogenase activity suggesting possible translational and posttranscriptional effects on ferritin expression.

77 NAL Call. No.: QK710.P62 Forcing expression of a soybean root glutamine synthetase gene in tobacco leaves induces a native gene encoding cytosolic enzyme. Hirel, B.; Marsolier, M.C.; Hoarau, A.; Hoarau, J.; Brangeon, J.; Schafer, R.; Verma, D.P.S.
Dordrecht : Kluwer Academic Publishers; 1992 Oct. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 20 (2): p. 207-218; 1992 Oct. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Multiple genes; Structural genes; Glutamate-ammonia ligase; Promoters; Gene expression; Transgenics; Genetic transformation; Root nodules; Roots; Genetic regulation; Ammonia; Leaves; Cytoplasm; Immunocytochemistry; Cytosol; Messenger RNA; Nucleotide sequences

Abstract: Glutamine synthetase (GS; EC 6.3.1.2) is present in different subcellular compartments in plants. It is located in the cytoplasm in root and root nodules while generally present in the chloroplasts in leaves. The expression of GS gene(s) is enhanced in root nodules and in soybean roots treated with ammonia. We have isolated four genes encoding subunits of cytosolic GS from soybean (Glycine max L. cv. Prize). Promoter analysis of one of these genes (GS15) showed that it is expressed in a root-specific manner in transgenic tobacco and Lotus corniculatus, but is induced by ammonia only in the legume background. Making the GS15 gene expression constitutive by fusion with the CaMV-35S promoter led to the expression of GS in the leaves of transgenic tobacco plants. The soybean GS was functional and was located in the cytoplasm in tobacco leaves where this enzyme is not normally present. Forcing this change in the location of GS caused concomitant induction of the mRNA for a native cytosolic GS in the leaves of transgenic tobacco. Shifting the subcellular location of GS in transgenic plants apparently altered the nitrogen metabolism and forced the induction in leaves of a native GS gene encoding a cytosolic enzyme. The latter is normally expressed only in the root tissue of tobacco. This phenomenon may suggest a hitherto uncharacterized metabolic control on the expression of certain genes in plants.

78 NAL Call. No.: 450 P699 Freezing tolerance and alteration of translatable mRNAs in alfalfa (Medicago sativa L.) Hardened at subzero temperatures. Castonguay, Y.; Nadeau, P.; Laberge, S. Kyoto : Japanese Society of Plant Physiologists; 1993 Jan. Plant and cell physiology v. 34 (1): p. 31-38; 1993 Jan. Includes references.

Language: English

Descriptors: Medicago sativa; Cold hardening; Freezing; Cold tolerance; Stress response; Gene expression; Messenger RNA; Translation; Protein synthesis; Glycine; Cultivars; Regulation; Cold

Abstract: We analyzed changes in populations of translatable mRNAs occurring in crowns of the cold-tolerant alfalfa (Medicago sativa L.) cv. Apica (CT) and the cold-sensitive cv. CUF-101 (CS) after their acclimation at low nonfreezing temperatures and at subzero temperatures. Both cultivars showed very similar translation profiles under all treatments. Low temperatures induced significant changes in the populations of translatable mRNAs. We observed a relationship between the accumulation of cold-regulated (COR) translation products and freezing tolerance within cultivars. Moreover, at least three COR translation products were specific to the CT and might be related to hardiness potential in alfalfa. Whereas extension of the cold acclimation period at 2 degrees C reduced cold tolerance, incubation at subzero temperatures increased or maintained freezing tolerance. This increased hardiness was associated with enhanced translation of COR polypeptides and also with the appearance of new translatable mRNAs. This is, to our knowledge, the first report of altered gene expression in plants incubated at subzero temperatures. Marked changes in populations of translatable mRNAs at temperatures below freezing might be related to previous reports that alfalfa achieves maximum hardiness under snow cover when the soil has frozen. Translation in the presence of [3H]glycine showed that a large proportion of the COR genes encode for glycine-rich proteins (GRPs) and that some of the GRPs are specific to the CT.

79 NAL Call. No.: 450 P692 Frost, abscisic acid, and desiccation hasten embryo development in Brassica napus.
Johnson-Flanagan, A.M.; Huiwen, Z.; Geng, X.M.; Brown, D.C.W.; Nykiforuk, C.L.; Singh, J.
Rockville, Md. : American Society of Plant Physiologists; 1992 Jun. Plant physiology v. 99 (2): p. 700-706; 1992 Jun. Includes references.

Language: English

Descriptors: Brassica napus; Plant embryos; Seed development; Regulation; Abscisic acid; Frost; Desiccation; Seed germination; Plant proteins; Transcription; Gene expression

Abstract: Seed development in canola (Brassica napus) following a mild nonlethal freeze was examined with respect to abscisic acid (ABA) levels, desiccation, and expression of LEA.76 and isocitrate lyase (ICL) transcripts. Plants with seed of 70 and 55% moisture contents were frozen to -5 degrees C for 3 hours, and seed development followed after thawing. In addition, similar processes were compared during induction of extreme desiccation tolerance by application of ABA in Brassica microspore-derived haploid embryos in culture. A mild freeze/thaw caused a premature switch in seed developmental direction from predesiccation to desiccation as indicated by an immediate and accelerated loss of seed moisture to levels similar to the mature seed in 7 instead of 35 days, and by elevated ABA levels and induction of low levels of LEA.76 and ICL transcripts. Similarly, addition of ABA to haploid embryos in culture resulted in the induction of desiccation tolerance and low levels of late embryogenesis-abundant (LEA) but not ICL transcripts. In contrast, normal seed development and desiccation of ABA-treated (desiccation-tolerant) embryos resulted in the induction of ICL and very high levels of LEA.76 transcripts. Similarly, desiccation of control (desiccation-sensitive) embryos resulted in very high levels of LEA.76 transcripts. These results indicate that although LEA-type proteins have been implicated in the development of desiccation tolerance, high transcript levels of LEA.76 were not observed in the induction of desiccation tolerance either by a hastening of the maturation process in the developing Brassica seed, or by the exogenous application of ABA to Brassica haploid embryos in culture.

80 NAL Call. No.: S494.5.B563C87 Functional and structural analysis of promoter fragments in soybean nuclear DNA.
Dong, J.L.; Xu, X.L.; Sakai, F.; Li, J.L. Dordrecht : Kluwer Academic Publishers; 1993. Current plant science and biotechnology in agriculture v. 15: p. 165-168; 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.

Language: English

Descriptors: Glycine max; Glycyrrhiza glabra; Promoters; Recombinant DNA; Beta-glucuronidase; Genetic transformation; Gene expression; Histoenzymology; Reporter genes

81 NAL Call. No.: 500 N21P Gene expression in cotton (Gossypium hirsutum L.) fiber: cloning of the mRNAs. John, M.E.; Crow, L.J.
Washington, D.C. : The Academy; 1992 Jul01. Proceedings of the National Academy of Sciences of the United States of America v. 89 (13): p. 5769-5773; 1992 Jul01. Includes references.

Language: English

Descriptors: Gossypium hirsutum; Messenger RNA; Cloning; Gene expression; Nucleotide sequences; Amino acid sequences; Dna libraries; Transgenics

Abstract: Cotton, an important natural fiber, is a differentiated epidermal cell. The number of genes that are active in fiber cells is similar to those in leaf, ovule, or root tissues. Through differential screening of a fiber cDNA library, we isolated five cDNA clones that are preferentially expressed in fiber. One of the cDNA clones, pCKE6, corresponded to an abundant mRNA in fiber. Transcripts for E6 were detected throughout the development of the fiber. Immunoprecipitation of in vitro translation products and Western blot analysis of fiber proteins showed two polypeptides in the range of 30-32 kDa as the products of E6 mRNA. Sequence analysis and hybrid-selected RNA translation also suggest that E6 mRNAs encode two polypeptides. Concentrations of E6 mRNA and protein are highest during the late primary cell wall and early secondary cell wall synthesis stages. Sequence comparison of E6 with other known eukaryotic and prokaryotic genes reveals no significant homology (Genbank; December 1991). E6 or a homologous gene(s) is conserved in several members of Malvaceae as well as in one other fiber-producing plant, kapok, but is not found in several other plants examined or in Acetobacter xylinum. A genomic clone corresponding to pCKE6 was isolated, and the promoter element of the E6 gene was shown to direct the expression of a carrot extensin mRNA in a tissue-specific and developmentally regulated fashion in transgenic cotton plants.

82 NAL Call. No.: 450 P692 A gene that encodes a proline-rich nodulin with limited homology to PsENOD12 is expressed in the invasion zone of Rhizobium meliloti-induced alfalfa root nodules.
Lobler, M.; Hirsch, A.M.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Sep. Plant physiology v. 103 (1): p. 21-30; 1993 Sep. Includes references.

Language: English

Descriptors: Medicago sativa; Amino acid sequences; Gene expression; Genetic code; Nucleotide sequences; Nodulins; Proline; Rhizobium meliloti; Root nodules; Transcription

Abstract: To define the early stages of the interaction between Rhizobium and host legumes, we have cloned and characterized three early nodulin-encoding sequences from an alfalfa (Medicago sativa L.) cDNA library by probing with a fragment of a cDNA clone for PsENOD12, an infection-related nodulin from pea (Pisum sativum L). Although the coding regions of the three clones are 95 to 98% homologous to each other, they are only 43% homologous to the pea clone. However, the putative signal peptide encoded by the alfalfa cDNA clones is 100% homologous to the PsENOD12 signal peptide. The spatial and temporal expression patterns of PsENOD12 and the alfalfa clones were compared. In situ hybridization experiments detected RNA transcripts in the invasion zone of mature nitrogen-fixing nodules, the same site where PsENOD12 mRNAs are found. Transcripts were also found by in situ hybridization in cells of Rhizobium meliloti exoH mutant-induced nodules penetrated by infection threads, but northern analysis did not detect transcripts in Inf- (infection thread minus) nodules elicited by R. meliloti exoB nodules or in pseudonodules elicited by treatment with the auxin transport inhibitor N-1-(naphthyl)phthalamic acid. In addition, the alfalfa gene represented by these cDNA clones exhibited a temporal expression pattern that differed from that of PsENOD12, which is transiently expressed. These data, plus information derived from Southern blot analysis, indicate that we have isolated cDNA clones for a novel early nodulin, which we have designated MsENOD10 (Medicago sativa Early Nodulin 10).

83 NAL Call. No.: 450 P5622 Genetic and chemical polymorphisms of saponins in soybean seed. Tsukamoto, C.; Kikuchi, A.; Harada, K.; Kitamura, K.; Okubo, K. Oxford ; New York : Pergamon Press, 1961-; 1993 Nov. Phytochemistry v. 34 (5): p. 1351-1356; 1993 Nov. Includes references.

Language: English

Descriptors: Glycine max; Seeds; Triterpenoid saponins; Structure; Biochemical polymorphism; Genetic polymorphism; Gene expression; Inheritance

Abstract: The variation in saponin composition in soybean seeds is explained by different combinations of five genes controlling the utilization of soyasapogenol glycosides as substrates. The function of these genes is variety-specific and organ-specific. Phenotypes of over 1000 soybeans were classified into eight saponin types, and the frequency of phenotypes was different between the cultivated [Glycine max (L.) Merr.] and the wild soybean (G. soja Sieb. & Zucc.). The AaBc saponin type predominated in G. soja (58.4% of test collections), but was only found in 0.3% of G. max. Four unidentified arabinoside saponins were detected in the seeds of the AaBc type soybeans.The mode of inheritance of saponin types is explained by a combination of co-dominant, dominant and recessive acting genes. The combined chemical and genetic data show that the directed manipulation of soybean saponin composition is a possibility for the future.

84 NAL Call. No.: 511 P444AEB Genetic transformation of alfalfa using the Ti plasmid system of Agrobacterium tumefaciens.
Deineko, E.V.; Rivkin, M.I.; Komarova, M.L.; Vershinin, A.V.; Shumnyi, A.V.K. New York, N.Y. : Consultants Bureau; 1992 Jan. Doklady : biological sciences - Akademiia nauk SSSR v. 319 (1/6): p. 457-459. ill; 1992 Jan. Translated from: Doklady Akademii Nauk SSSR, v. 319 (6), 1991, p. 1473-1476. (511 P444A). Includes references.

Language: English; Russian

Descriptors: Medicago sativa; Gene expression; Genetic transformation; Plasmids; Transgenics; Agrobacterium tumefaciens

85 NAL Call. No.: QK710.P62 The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by a gene family.
Xue, J.; Lenman, M.; Falk, A.; Rask, L. Dordrecht : Kluwer Academic Publishers; 1992 Jan. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (2): p. 387-398; 1992 Jan. Includes references.

Language: English

Descriptors: Sinapis alba; Brassica napus; Arabidopsis thaliana; Multigene families; Thioglucosidase; Nucleotide sequences; Gene expression; Messenger RNA; Amino acid sequences

Abstract: A full-length cDNA clone (MB3) and three partial clones (MA1, MB1 and MB2) which encode myrosinase (thioglucoside glucohydrolase, EC 3.2.3.1) were isolated from a Sinapis alba (white mustard) cDNA library. Nucleotide sequence analysis of these clones revealed that they are encoded by a gene family. Southern blot analysis with gene-specific probes showed that the gene family consists of a least two subfamilies (MA and MB) each with several members both in S. alba and in Brassica napus (oilseed rape). In Arabidopsis thaliana (wall cress) only three myrosinase genes seem to be present. Northern blot analysis indicated that all the myrosinase mRNA species have the same size, approximately 1.95 kb.

86 NAL Call. No.: 500 N21P Guanine nucleotide binding protein involvement in early steps of phytochrome-regulated gene expression.
Romero, L.C.; Lam, E.
Washington, D.C. : The Academy; 1993 Feb15. Proceedings of the National Academy of Sciences of the United States of America v. 90 (4): p. 1465-1469. ill; 1993 Feb15. Includes references.

Language: English

Descriptors: Glycine max; Binding proteins; Gene expression; Guanine; Nucleotides; Phytochrome; Toxins; Transcription

Abstract: The transmission process of light signals from plant photoreceptors to target cellular events is largely unknown. In the present work, we show that treatment of dark-adapted soybean cells (SB-P) with cholera toxin or pertussis toxin uncouples phytochrome-dependent gene expression. Addition of as little as 10 ng of toxin per ml is sufficient to activate expression of genes encoding the major chlorophyll a/b-binding protein (cab) in the dark. Significant levels of cab transcript accumulation are detected within 0.5 h after addition of the toxins and expression of these genes is desensitized to further light treatments. Treatment of SB-P cells with the calmodulin antagonist N-(6-aminobexyl)-5-chloro-1-naphthalenesulfonamide hydrochloride (W-7) prevents induction of the photoregulated gene by phytochrome or bacterial toxins. These results indicate the involvement of guanine nucleotide binding protein(s) in phytochrome-mediated cab gene activation. A likely site of action for this step is between the photoreceptor and a downstream W-7-sensitive effector.

87 NAL Call. No.: 442.8 Z34 Haploid and diploid expression of a Brassica campestris anther-specific gene promoter in Arabidopsis and tobacco.
Xu, H.; Davies, S.P.; Kwan, B.Y.H.; O'Brien, A.P.; Singh, M.; Knox, R.B. Berlin, W. Ger. : Springer International; 1993 May. Molecular & general genetics : MGG v. 239 (1/2): p. 58-65; 1993 May. Includes references.

Language: English

Descriptors: Brassica campestris; Promoters; Structural genes; Plant proteins; Anthers; Nucleotide sequences; Amino acid sequences; Multigene families; Recombinant DNA; Reporter genes; Beta-glucuronidase; Gene expression; Histoenzymology; Genetic transformation; Transgenic plants; Pollen; Nicotiana tabacum; Arabidopsis thaliana; Complementary DNA

Abstract: The anther-specific cDNA clone Bcp1 from Brassica campestris is expressed in both the haploid pollen and diploid tapetum, as shown by in situ hybridization. We have isolated Bgp1, a genomic clone homologous to Bcp1. The coding region and extensive 5' flanking sequences of Bgp1 have been sequenced, and the coding region shows 88% identity with Bcp1. RNA gel blot analysis confirmed the expression of Bgp1-specific transcripts in B. campestris pollen. A 767 bp 5' DNA fragment was fused to the reporter gene beta-glucuronidase (gus) and introduced into both Arabidopsis thaliana and Nicotiana tabacum by transformation. This 5' fragment directed high-level expression in the pollen and tapetum of transgenic Arabidopsis. In transgenic tobacco however, the same construct was expressed only in pollen. A series of 5' deletion constructs has been created and used to transform A. thaliana to analyse the 5' region of Bgp1. The results indicate that Bgp1 expression in the tapetum and pollen of Arabidopsis requires the presence of different 5' DNA sequences.

88 NAL Call. No.: 442.8 Z34 High frequency, heat treatment-induced inactivation of the phosphinothricin resistance gene in transgenic single cell suspension cultures of Medicago sativa.
Walter, C.; Broer, I.; Hillemann, D.; Puhler, A. Berlin, W. Ger. : Springer International; 1992 Nov. M G G : Molecular and general genetics v. 235 (2/3): p. 189-196; 1992 Nov. Includes references.

Language: English

Descriptors: Medicago sativa; Genetic transformation; Transgenics; Structural genes; Acyltransferases; Glufosinate; Herbicide resistance; Gene expression; Cell suspensions; Genetic regulation; Heat; Callus; Regenerative ability; Enzyme activity

Abstract: One descendant of the Medicago sativa Ra-3 transformant T304 was analysed with respect to the somatic stability of the synthetic phosphinothricin-N-acetyltransferase (pat) gene which was used as a selective marker and was under the control of the 5'/3' expression signals of the cauliflower mosaic virus (CaMV) gene VI. In order to quantify gene instability, we developed a system for culturing and regenerating individual cells. Single cell suspension cultures derived from T304 and the ancestral non-transgenic M. sativa cultivar Ra-3, were established. The cells were regenerated into monoclonal calli. In transgenic calli, the phosphinothricin (Pt)-resistance phenotype was retained after more than 2 months of non-selective growth. In contrast, up to 12% of the suspension culture cells grown under non-selective conditions and at constant temperature (25 degrees C) lost the herbicide-resistance phenotype within 150 days. Surprisingly, a heat treatment (37 degrees C), lasting for 10 days, during the culture period resulted in an almost complete (95%) loss of the Pt resistance of the suspension culture cells. However, the frequency of cell division was identical in cultures grown under normal and heat treatment conditions. A biochemical test revealed that no phosphinothricin-N-acetyltransferase activity was present in heat treated, Pt-sensitive cells. The resistance level of the Pt-sensitive transgenic cells was equivalent to that of the wild-type cells. A PCR analysis confirmed the presence of the pat gene in heat treated, Pt-sensitive cells. From these results it is concluded that the Pt resistance gene was heat-inactivated at a high frequency in the M. sativa suspension cultures.

89 NAL Call. No.: 381 J824 Histone synthesis and turnover in alfalfa. Fast loss of highly acetylated replacement histone variant H3.2.
Waterborg, J.H.
Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993 Mar05.
The Journal of biological chemistry v. 268 (7): p. 4912-4917; 1993 Mar05. Includes references.

Language: English

Descriptors: Medicago varia; Histones; Protein synthesis; Chemical reactions; Chromatin; Gene expression; Structural genes; Transcription

Abstract: Histone synthesis in alfalfa tissue culture cells was studied by labeling with tritiated lysine, purification of histone proteins by reversed-phase high pressure liquid chromatography, and fluorography of acid/urea/Triton X-100 polyacrylamide gels. Minor histone variant H3.2 was synthesized twice as fast as major variant H3.1. The predicted difference in histone H3 variant turnover was examined during continued growth. More than 50% of newly synthesized histone H3.2 and 20% of new H3.1 were lost from chromatin over a period of 100 h. This produced a ratio between the stable remaining portions of each new histone H3 variant protein identical to that of the steady-state histone H3 variants. The labile portion of new histone H3.2 (half-life of 20 h) was rapidly lost specifically from transcriptionally active chromatin as judged by the acetylation level of nearly 1.5 acetylated lysines/histone molecule, a level 50% higher than the acetylation in histone H3.2 overall and three times that of histone H3.1. These results and the constitutive level of H3.2 gene expression identify histone H3.2 of alfalfa as a functional replacement histone variant. The extent of its preferential assembly into active chromatin nucleosomes and the rapid rate of its subsequent loss indicate significant dissolution of plant nucleosomes during gene transcription.

90 NAL Call. No.: QK725.P532 Identification of a methyl jasmonate-responsive domain in the soybean vspB promoter.
Mason, H.S.; DeWald, D.B.; Mullet, J.E. Rockville, Md. : American Society of Plant Physiologists; 1993 Mar. The Plant cell v. 5 (3): p. 241-251; 1993 Mar. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Promoters; Acid phosphatase; Recombinant DNA; Reporter genes; Beta-glucuronidase; Gene expression; Genetic regulation; Jasmonic acid; Derivatives; Sucrose; Abiotic injuries; Deletions; Nucleotide sequences; Genetic transformation; Transgenic plants; Histoenzymology; Plant

Abstract: Soybean vspB encodes a highly expressed vegetative storage protein-acid phosphatase. In soybean, vspB expression is stimulated by methyl jasmonate (MeJA) and sugars. The vspB promoter was studied by transforming tobacco with fusions of 5' noncoding vspB DNA and the gene encoding beta-glucuronidase (GUS). Constructs containing 833 bp of vspB 5' DNA showed high expression of GUS in stems, leaf veins and trichomes, sepals, and pollen. Sucrose (0.2 M) and MeJA (10(-5) M) increased gene expression when applied to leaf tissue. Deletion of the region -787 to -520 with respect to the transcription initiation site rendered the vspB promoter noninducible by MeJA but still sucrose responsive. This result indicates that DNA elements capable of modulating vspB by MeJA can be separated from carbon response elements. Further 5' end deletion from -520 to -403 or 3' end deletion from -165 to -289 removed DNA sequences involved in carbon modulation of gene expression. A DNA domain that mediates the MeJA response was further localized to a 50-bp region between -535 and -585. This domain when fused to a cauliflower mosaic virus (CaMV) 35S truncated (-88) promoter makes the CaMV promoter responsive to MeJA. The MeJA-responsive domain contains a G-box motif (CACGTG) and a C-rich sequence. A similar 50-bp DNA region is present in the putative promoter of vspA. Related sequences are located in a wound- and MeJA-responsive domain of the proteinase inhibitor II gene and a UV-responsive promoter domain of chs, the gene encoding chalcone synthase that is also responsive to MeJA.

91 NAL Call. No.: QK710.P62 Identification of two alfalfa early nodulin genes with homology to members of the pea Enod12 gene family.
Allison, L.A.; Kiss, G.B.; Bauer, P.; Poiret, M.; Pierre, M.; Savoure, A.; Kondorosi, E.; Kondorosi, A.
Dordrecht : Kluwer Academic Publishers; 1993 Jan. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 21 (2): p. 375-380; 1993 Jan. Includes references.

Language: English

Descriptors: Medicago sativa; Structural genes; Multigene families; Nodulins; Nucleotide sequences; Amino acid sequences; Gene expression; Nodulation; Root nodules

Abstract: In a search for plant genes expressed during early symbiotic interactions between Medicago sativa and Rhizobium meliloti, we have isolated and characterized two alfalfa genes which have strong sequence similarity to members of the Enod12 gene family of Pisum sativum. The M. sativa genes, MsEnod12A and B, encode putative protein products of 8066 Da and 12849 Da, respectively, each with a signal sequence at the N-terminus followed by a repetitive proline-rich region. Based on their expression during the initial period of nodule development, MsEnod12A and B are alfalfa early nodulin genes.

92 NAL Call. No.: S494.5.B563C87 Induction of genes encoding phenylpropanoid biosynthetic enzymes in soybean roots inoculated with B. japonicum, requires NOD gene induction and occurs independent of any known host functions. Estabrook, E.; Potenza, C.; Feder, A.I.; Sengupta-Gopalan, C. Dordrecht : Kluwer Academic Publishers; 1993. Current plant science and biotechnology in agriculture v. 14: p. 385-389; 1993. In the series analytic: Advances in molecular genetics of plant-microbe interactions. 2 / edited by E.W. Nester, and D.P.S. Verma. Proceedings of the 6th International Symposium on Molecular Plant-Microbe Interactions held July 1992, Seattle, Washington. Includes references.

Language: English

Descriptors: Glycine max; Bradyrhizobium japonicum; Gene expression; Structural genes; Phenylalanine ammonia-lyase; Chalcone isomerase; Naringenin-chalcone synthase; Genetic regulation; Roots; Nodulation; Cell differentiation; Root nodules; Root hairs; Messenger RNA

93 NAL Call. No.: SB732.6.M65 Isoflavonoid accumulation and expression of defense gene transcripts during the establishment of vesicular-arbuscular mycorrhizal associations in roots of Medicago truncatula.
Harrison, M.J.; Dixon, R.A.
St. Paul, MN : APS Press, [c1987-; 1993 Sep. Molecular plant-microbe interactions : MPMI v. 6 (5): p. 643-654; 1993 Sep. Includes references.

Language: English

Descriptors: Medicago truncatula; Medicago sativa; Glomus versiforme; Vesicular arbuscular mycorrhizas; Roots; Gene expression; Messenger RNA; Phenylalanine ammonia-lyase; Naringenin-chalcone synthase; Oxidoreductases; Medicarpin; Biosynthesis; Isoflavones; Flavonoids

94 NAL Call. No.: QK710.P62 The isolation and characterisation of a cDNA clone encoding L-asparaginase from developing seeds of lupin (Lupinus arboreus). Lough, T.J.; Reddington, B.D.; Grant, M.R.; Hill, D.F.; Reynolds, P.H.S.; Farnden, K.J.F.
Dordrecht : Kluwer Academic Publishers; 1992 Jun. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (3): p. 391-399; 1992 Jun. Includes references.

Language: English

Descriptors: Lupinus arboreus; Dna; Structural genes; Asparaginase; Nucleotide sequences; Amino acid sequences; Genetic code; Transcription; Gene expression; Messenger RNA; Seed development

Abstract: An L-asparaginase cDNA clone, BR4, was isolated from a Lupinus arboreus Sims developing seed expression library by screening with polyclonal antibodies to the seed asparaginase. The cDNA hybridised with an oligonucleotide probe designed from amino acid sequence data and was found on sequencing to be 947 bp in length. Six polypeptide sequences obtained previously could be placed along the longest open reading frame. Computer-aided codon use analysis revealed that the cDNA sequence was consistent with other plant genes in terms of codon use. The cDNA insert was used to analyse asparaginase transcription in various tissues by northern blot analysis. A transcript size of approximately 1.2 kb was detected in L. arboreus seed total and poly(A)+ RNA. The level of this transcript declined from 30 days after anthesis to an undetectable level by day 55. Furthermore, under the high stringency conditions used, the seed asparaginase cDNA did not hybridise with total or poly(A)+ RNA isolated from root tips, suggesting that the asparaginase known to be present in this tissue may be the product of a different gene. Southern analysis suggested the seed asparaginase is a single-copy gene. The plant asparaginase amino acid sequence did not have any significant homology with microbial asparaginases but was 23% identical and 66% similar (allowing for conservative substitutions) to a human glycosylasparaginase.

95 NAL Call. No.: 442.8 Z34 Isolation and characterization of novel nodulin cDNAs representig genes expressed at early stages of soybean nodule development. Kouchi, H.; Hata, S.
Berlin, W. Ger. : Springer International; 1993 Apr. M G G : Molecular and general genetics v. 238 (1/2): p. 106-119; 1993 Apr. Includes references.

Language: English

Descriptors: Glycine max; Bradyrhizobium japonicum; Complementary DNA; Nodulins; Nucleotide sequences; Amino acid sequences; Root nodules; Cell differentiation; Gene expression; Messenger RNA; Spatial distribution; Roots; Epidermis; Stems

Abstract: We took advantage of a subtractive hybridization procedure to isolate a set of cDNA clones of nodule-specific genes (nodulin genes) from developing soybean root nodules. Single-stranded 32P-labelled cDNA synthesized from nodule poly(A)+ RNA was hybridized with a large excess of uninfected root poly(A)+ RNA. Unhybridized cDNA was selected and used to screen nodule cDNA libraries. By this procedure we isolated several novel nodulin cDNA clones together with most of the nodulin cDNAs previously described. Four novel nodulin genes, which were expressed long before the onset of nitrogen fixation, were further characterized. GmN 6 and GmN 3 transcripts appeared in the roots less than 3 days after sowing and inoculation with Bradyrhizobium, but GmN 6 transcripts were also detected at very low levels in the stems of uninfected plants. Transcripts of GmN 15 and GmN 0 first appeared at 6-7 days, just before nodule emergence. Amino acid sequences of the predicted products of GmN 6, GmN 3 and GmN 0 exhibited no significant homology to proteins identified so far. The GmN 15 encoded protein has a limited but significant homology to some plant cyanins, suggesting that it is a metal-binding glycoprotein. In situ hybridization studies revealed that GmN 6 transcripts first appeared in the pericycle cells of the root stele near the infected site. During nodule emergence they were found in a few cell layers surrounding the vascular strands connecting the nodule meristem with the root stele, and in mature nodules they were present specifically in the pericycle cells in vascular bundles. These observations led us to hypothesize that GmN 6 gene products play a role in the transport and/or degradation of photosynthate. On the other hand, GmN 3 transcripts first appeared in the primary nodule meristem just below the root epidermis. In mature nodules they were only present in the infected cells.

96 NAL Call. No.: QK710.P62 Isolation and characterization of three families of auxin down-regulated cDNA clones.
Datta, N.; LaFayette, P.R.; Kroner, P.A.; Nagao, R.T.; Key, J.L. Dordrecht : Kluwer Academic Publishers; 1993 Mar. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 21 (5): p. 859-869; 1993 Mar. Includes references.

Language: English

Descriptors: Glycine max; Complementary DNA; Multigene families; Gene expression; Genetic regulation; Auxins; Nucleotide sequences; Amino acid sequences; Light; Plant proteins; Transcription; Messenger RNA; Plant development

Abstract: Five cDNA clones (ADR6, ADR11-1, ADR11-2, ADR12-1 and ADR12-2), representing three families of auxin down-regulated (ADR) genes were isolated and characterized. These were isolated by screening a lambdaZap cDNA library with the partial cDNA clones p6, p11 and p12, isolated earlier (Baulcombe and Key, J Biol Chem 255: 8907-8913, 1980). Hybrid-select translation of ADR6, ADR11-2 and ADR12-2 clones produced polypeptides of 33 kDa 22.5 kDa and a 6 and 7 kDa respectively, when analyzed by SDS-PAGE. ADR6 and ADR12-2 gave one and two spots, respectively, on an IEF-SDS 2D gel. ADR11-2 probably encodes a basic protein as it was only resolved on non-equilibrium pH gradient gel electrophoresis (NEPHGE). Genomic Southern blot analysis of ADR6, ADR11 and ADR12 suggests that each represents a small multigene family. The RNA levels corresponding to ADR6, ADR11 and ADR12 decrease in response to applied auxin by 100-, 15- and 10-fold, respectively (Baulcombe and Key, 1980). Runoff transcription, done in the presence and absence of auxin, showed that the rate of transcription of the genes corresponding to ADR6, ADR11-2 and ADR12-2 was reduced in the presence of auxin, but the decrease was small relative to the decrease in the cytoplasmic levels of these mRNAs, in response to auxin. A comparative analysis of the influence of auxin on in vitro transcription and steady state RNA levels corresponding to these ADR cDNAs suggests that the decrease in rate of transcription due to auxin is not enough to account for the auxin-induced decrease in the steady state levels. Northern analysis showed developmental and organ/tissue-specific response of these ADR genes. Furthermore, the expression of the genes corresponding to ADR6 and ADR12-1 appears to be up-regulated by light, whereas the gene corresponding to ADR11 appears to be down-regulated by light.

97 NAL Call. No.: QK710.P62 Isolation and characterization of two Brassica napus embryo acyl-ACP thioesterase cDNA clones.
Loader, N.M.; Woolner, E.M.; Hellyer, A.; Slabas, A.R.; Safford, R. Dordrecht : Kluwer Academic Publishers; 1993 Nov. Plant molecular biology v. 23 (4): p. 769-778; 1993 Nov. Includes references.

Language: English

Descriptors: Brassica napus; Complementary DNA; Multigene families; Thiolester hydrolases; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Enzyme precursors; Seeds; Plant embryos

Abstract: Acyl-ACP thioesterases are involved in regulating chain termination of fatty systems. Previously, acyl-ACP thioesterase purified from Brassica napus seed tissue has been shown to have a high preference for hydrolysing oleoyl-ACP. Here, oligonucleotides derived from B. napus oleoyl-ACP thioesterase protein sequence data have been used to isolate two acyl-ACP thioesterase clones from a B. napus embryo cDNA library. The two clones, pNL2 and pNL3, contain 1642 bp and 1523 bp respectively and differ in the length of their 3' non-coding regions. Both cDNAs contain open reading frames of 366 amino acids which encode for 42 kDa polypeptides. Mature rape thioesterase has an apparent molecular weight of 38 kDa on SDS-PAGE and these cDNAs therefore encode for precursor forms of the enzyme. This latter finding is consistent with the expected plastidial location of fatty acid synthase enzymes. Northern blot analysis shows thioesterase mRNA size to be ca. 1.6 kb and for the thioesterase genes to be highly expressed in seed tissue coincident with the most active phase of storage lipid synthesis. There is some sequence heterogeneity between the two cDNA clones, but overall they are highly homologous sharing 95.7% identity at the DNA level and 98.4% identity at the amino acid level. Some sequence heterogeneity was also observed between the deduced and directly determined thioesterase protein sequences. Consistent with the observed sequence heterogeneity was Southern blot data showing B. napus thioesterase to be encoded by a small multi-gene family.

98 NAL Call. No.: QK710.P62 The isolation and functional characterisation of a B. napus acyl carrier protein 5' flanking region involved in the regulation of seed storage lipid synthesis.
Silva, J. de; Robinson, S.J.; Safford, R. Dordrecht : Kluwer Academic Publishers; 1992 Apr. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (6): p. 1163-1172; 1992 Apr. Includes references.

Language: English

Descriptors: Brassica napus; Nicotiana tabacum; Agrobacterium tumefaciens; Genes; Promoters; Plant proteins; Lipogenesis; Nucleotide sequences; Gene expression; Seeds; Reporter genes; Beta-glucuronidase; Transgenics; Genetic transformation; Genetic regulation; Seed development; Histoenzymology

Abstract: Acyl carrier protein (ACP) is a key component of the fatty acid biosynthetic machinery in plants. A 1.4 kb 5' flanking region of a Brassica napus ACP gene (ACP05) was transcriptionally fused to the reporter gene beta-glucuronidase (GUS), and expression of the chimaeric gene monitored in transgenic tobacco. GUS activity was found to increase through seed development reaching a maximum value, coincident with the most active phase of storage lipid synthesis that was, on average, 100-fold higher than that observed in leaf. In control plants transformed with CaMV 35S-GUS constructs, GUS activity was similar in leaf and all stages of seed development. Based on average values, the level of GUS expression obtained via the ACP promoter was comparable to that obtained from the CaMV 35S promoter. We therefore conclude that the isolated 5' ACP flanking sequence represents a strong promoter element involved in the developmental regulation of storage lipid synthesis in B. napus seed tissue. Putative regulatory elements in the 5' upstream region of ACP05 were identified by dot matrix analysis and by sequence comparison with the upstream regions from a second seed-expressed rape ACP gene and from an Arabidopsis ACP gene.

99 NAL Call. No.: QK745.J6 Jasmonate-induced proteins in cotton: immunological relationship to the respective barley proteins and homology of transcripts to late embryogenesis abundant (Lea) mRNAs.
Reinbothe, S.; Machmudova, A.; Wasternack, C.; Reinbothe, C.; Parthier, B. New York, N.Y. : Springer; 1992.
Journal of plant growth regulation v. 11 (1): p. 7-14; 1992. Includes references.

Language: English

Descriptors: Gossypium hirsutum; Cotyledons; Protein synthesis; Induction; Jasmonic acid; Genetic regulation; Gene expression; Messenger RNA; Transcription; Hordeum vulgare; Plant proteins; Embryogenesis; Plant embryos

100 NAL Call. No.: 500 N21P Jasmonic acid/methyl jasmonate accumulate in wounded soybean hypocotyls and modulate wound gene expression.
Creelman, R.A.; Tierney, M.L.; Mullet, J.E. Washington, D.C. : The Academy; 1992 Jun01. Proceedings of the National Academy of Sciences of the United States of America v. 89 (11): p. 4938-4941. ill; 1992 Jun01. Includes references.

Language: English

Descriptors: Glycine max; Hypocotyls; Injuries; Jasmonic acid; Cellular biology; Cell wall components; Gene expression; Plant proteins; Proline

Abstract: Jasmonic acid (JA) and its methyl ester, methyl jasmonate (MeJA), are plant lipid derivatives that resemble mammalian eicosanoids in structure and biosynthesis. These compounds are proposed to play a role in plant wound and pathogen responses. Here we report the quantitative determination of JA/MeJA in planta by a procedure based on the use of [13C,2H3]MeJA as an internal standard. Wounded soybean (Glycine max [L] Merr. cv. Williams) stems rapidly accumulated MeJA and JA. Addition of MeJA to soybean suspension cultures also increased mRNA levels for three wound-responsive genes (chalcone synthase, vegetative storage protein, and proline-rich cell wall protein) suggesting a role for MeJA/JA in the mediation of several changes in gene expression associated with the plants' response to wounding.

101 NAL Call. No.: QK710.P62 The legumin boxes and the 3' part of a soybean beta-conglycinin promoter are involved in seed gene expression in transgenic tobacco plants. Chamberland, S.; Daigle, N.; Bernier, F. Dordrecht : Kluwer Academic Publishers; 1992 Sep. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (6): p. 937-949; 1992 Sep. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana; Agrobacterium tumefaciens; Promoters; Plant proteins; Seeds; Nucleotide sequences; Controlling elements; Reporter genes; Beta-glucuronidase; Genetic transformation; Transgenics; Gene expression; Transcription; Mutants; Induced mutations; Genetic regulation; Plant embryos; Histoenzymology; Roots; Leaves

Abstract: beta-conglycinin is one of the major seed storage proteins in soybean. It is composed of three subunits, namely alpha, alpha' and beta. The expression of beta-conglycinin is highly regulated, being restricted to the embryo during the mid-maturation phase of embryogeny. Two series of constructs were made with the 2' subunit promoter and the GUS reporter gene to investigate the cis-acting elements involved in the regulated expression of this promoter. The activity of each construct was tested in transgenic tobacco plants. In the first series of constructs, we checked if the 'legumin box', a sequence found in most legume seed storage protein genes as well as in other seed-specific genes, is involved in the regulated expression of the alpha' subunit of the beta-conglycinin gene in tobacco. To this end, both copies of the alpha' subunit promoter legumin boxes were mutagenized in vitro. The transcriptional activity of the single mutants and the double mutant were compared with that of the wild-type promoter. Our results show that the legumin boxes act together to increase transcription of the beta-conglycinin alpha' subunit gene by about a factor of ten. This is the first demonstration of a function for the legumin box in transcriptional regulation. In the second series of experiments, we wished to determine if the 3' part of the promoter (the CCAAT and TATAA region) contains important regulatory elements. We found that this small fragment (-82 to +13 bp) can confer by itself a low level of seed-specific gene expression. Chimaeric promoters constructed from parts of the alpha' subunit promoter and of the constitutive CaMV 35S promoter were also analysed. These constructs also revealed the importance of the CCAAT and TATAA region of the alpha' subunit promoter in seed-specific gene expression.

102 NAL Call. No.: QK710.P68 Light- and sucrose-dependent gene expression in photomixotrophic cell suspension cultures and protoplasts of rape (Brassica napus L.). Harter, K.; Talke-Messerer, C.; Barz, W.; Schafer, E. 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. 507-516; 1993 Sep. Includes references.

Language: English

Descriptors: Brassica napus; Cell suspensions; Chlorophyll a/b binding protein; Gene expression; Growth; Light; Protoplasts; Sucrose

103 NAL Call. No.: QD341.A2N8 Metal-regulated transcription in eukaryotes. Thiele, D.J.
Oxford : IRL Press; 1992 Mar25.
Nucleic acids research v. 20 (17): p. 1183-1191; 1992 Mar25. Includes references.

Language: English

Descriptors: Saccharomyces cerevisiae; Torulopsis glabrata; Chlamydomonas reinhardtii; Glycine max; Phanerochaete chrysosporium; Mice; Rats; Transcription; Genetic regulation; Metal ions; Gene expression

104 NAL Call. No.: QK710.P62 Minimal enhancer elements of the leghemoglobin lba and lbc3 gene promoters from Glycine max L. have different properties. She, Q.; Lauridsen, P.; Stougaard, J.; Marcker, K.A. Dordrecht : Kluwer Academic Publishers; 1993 Sep. Plant molecular biology v. 22 (6): p. 945-956; 1993 Sep. Includes references.

Language: English

Descriptors: Glycine max; Lotus corniculatus; Promoters; Deletions; Leghemoglobin; Recombinant DNA; Reporter genes; Chloramphenicol acetyltransferase; Beta-glucuronidase; Gene expression; Genetic regulation; Genetic transformation; Transgenic plants; Histoenzymology; Roots; Root nodules

Abstract: The characteristics of the soybean leghemoglobin lba gene promoter were analyzed and important promoter elements from the lba and lbc3 promoters were compared using transgenic Lotus corniculatus plants. A 5' deletion analysis of the lba promoter delimited two cis-acting elements controlling expression: a distal positive element (-1254, -884) required for expression and a proximal element (-285, -60) essential for full-level activity. In contrast to the corresponding region of the lbc3 promoter, the lba proximal element is unable to control expression from the heterologous CaMV 35S enhancer. The upstream positive element of the lba gene contains a positionand orientation-independent enhancer between positions (-1091, -788). The sequence of this enhancer region is conserved in the lbc3 gene upstream -1333, -1132) of the previously assigned strong positive element (SPE; -1090, -947). The present analysis revealed some of the properties of this extended lbc3 SPE element. The extended element (-1364, -947) functions in both orientations from 5' locations whereas the SPE2 subcomponent (-1364, -1154) containing the conserved sequence is only active in the correct orientation. Removal of the SPE2 by internal deletion demonstrates that the SPE2 subcomponent is indispensable for the activity of the lbc3 upstream positive element. These results indicate that the upstream positive elements of the lba and lbc3 genes possess different properties although their conserved minimal enhancer sequence has similar function. This may reflect the differential expression of the two lb genes of Glycine max L.

105 NAL Call. No.: 500 N21P Modification of Brassica seed oil by antisense expression of a stearoly-acyl carrier protein desaturase gene.
Knutzon, D.S.; Thompson, G.A.; Radke, S.E.; Johnson, W.B.; Knauf, V.C.; Kridl, J.C.
Washington, D.C. : The Academy; 1992 Apr01. Proceedings of the National Academy of Sciences of the United States of America v. 89 (7): p. 2624-2628; 1992 Apr01. Includes references.

Language: English

Descriptors: Brassica campestris; Brassica napus; Gene expression; Genetic engineering; Lipid metabolism; Molecular genetics; Rapeseed oil; Saturated fatty acids; Biosynthesis

Abstract: Molecular gene transfer techniques have been used to engineer the fatty acid composition of Brassica rapa and Brassica napus (canola) oil. Stearoyl-acyl carrier protein (stearoyl-ACP) desaturase (EC 1.14.99.6) catalyzes the first desaturation step in seed oil biosynthesis, converting stearoyl-ACP to oleoyl-ACP. Seed-specific antisense gene constructs of B. rapa stearoyl-ACP desaturase were used to reduce the protein concentration and enzyme activity of stearoyl-ACP desaturase in developing rapeseed embryos during storage lipid biosynthesis. The resulting transgenic plants showed dramatically increased stearate levels in the seeds. A continuous distribution of stearate levels from 2% to 40% was observed in seeds of a transgenic B. napus plant, illustrating the potential to engineer specialized seed oil compositions.

106 NAL Call. No.: 442.8 Z34 Modulation of glutamine synthetase gene expression in tobacco by the introduction of an alfalfa glutamine synthetase gene in sense and antisense orientation: molecular and biochemical analysis. Temple, S.J.; Knight, T.J.; Unkefer, P.J.; Sengupta-Gopalan, C. Berlin, W. Ger. : Springer International; 1993 Jan. M G G : Molecular and general genetics v. 236 (2/3): p. 315-325; 1993 Jan. Includes references.

Language: English

Descriptors: Medicago sativa; Nicotiana tabacum; Structural genes; Complementary DNA; Glutamate-ammonia ligase; Genetic transformation; Transgenics; Antisense RNA; Genetic regulation; Gene expression; Transcription; Enzyme activity; Messenger RNA; Translation

Abstract: A glutamine synthetase (GS) cDNA isolated from an alfalfa cell culture cDNA library was found to represent a cytoplasmic GS. The full-length alfalfa GS1 coding sequence, in both sense and antisense orientation and under the transcriptional control of the cauliflower mosaic virus 35S promoter, was introduced into tobacco. Leaves of tobacco plants transformed with the sense construct contained greatly elevated levels of GS transcript and GS polypeptide which assembled into active enzyme. Leaves of the plants transformed with the antisense GS1 construct showed a significant decrease in the level of both GS1 and GS2 polypeptides and GS activity, but did not show any significant decrease in the level of endogenous GS mRNA. We have proposed that antisense inhibition using a heterologous antisense GS RNA occurs at the level of translation. Our results also suggest that the post-translational assembly of GS subunits into a holoenzyme requires an additional factor(s) and is under regulatory control.

107 NAL Call. No.: QK725.P56 1993 Molecular analysis of cytoplasmic male sterility in sunflower (Helianthus annuus).
Zetsche, K.; Horn, R.
Weinheim ; New York : VCH; 1993.
Plant mitochondria : with emphasis on RNA editing and cytoplasmic male sterility /. p. 411-422; 1993. Includes references.

Language: English

Descriptors: Helianthus annuus; Mitochondrial DNA; Cytoplasmic male sterility; Mitochondrial genetics; Inversion; Structural genes; Transcription; Gene expression; Molecular mapping

Abstract: The most thoroughly investigated CMS type in sunflower is the PET1 (or Leclercq) cytoplasm. The mtDNAs of male-sterile and fertile lines differ only in an area of about 17 kb. The rearranged region which is framed by the atpA gene and the cob gene includes an 11 kb inversion and an about 5 kb insertion. Due to the 5 kb insertion a new open reading frame (orfH522) is created downstream of the atpA gene. Northern hybridizations revealed that orfH522 is co-transcribed with the atpA gene on an additional larger transcript which can be observed only in the male-sterile lines. The 11 kb inversion seems to be also present in a minor subpopulation of mitochondrial DNA molecules of fertile H. petiolaris plants. The inversion may involve the 261 bp inverted repeat. Southern analyses indicate that the 5 kb insertion seems to be composed of sequences from the mitochondrial DNA, the nuclear genome and of sequences of yet unknown origin. Interesting in this connection is that a homology to the 5 kb insertion could also be detected in another male-sterile cytoplasm in sunflower, MAX1, although it is still unclear whether it plays a role in creating the CMS phenotype in this type of cytoplasm. Comparing the mitochondrially encoded in organello translation products of male-sterile and fertile lines, a 16 kD polypeptide could only be observed in the male-sterile lines. This protein which is membrane-bound was not detectable in fertile H. annuus and H. petiolaris.

108 NAL Call. No.: QK865.A1R4 Molecular biology of stress-induced phenylpropanoid and isoflavonoid biosynthesis in alfalfa.
Dixon, R.A.; Choudhary, A.D.; Dalkin, K.; Edwards, R.; Fahrendorf, T.; Gowri, G.; Harrison, M.J.; Lamb, C.J.; Loake, G.J.; Maxwell, C.A. New York, N.Y. : Plenum Press; 1992.
Recent advances in phytochemistry v. 26: p. 91-138; 1992. In the series analytic: Phenolic Metabolism in Plants / edited by H.A. Stafford and R.K. Ibrahim. Proceedings of the Thirty-first Annual Meeting of the Phytochemical Society of North America, June 1991, Fort Collins, Colorado. Literature review. Includes references.

Language: English

Descriptors: Medicago sativa; Propionic acid; Biosynthesis; Flavonoids; Biochemical pathways; Ligases; Transferases; Hydro-lyases; Enzyme activity; Genetic regulation; Transcription; Plant breeding; Literature reviews; Nucleotide sequences; Gene expression

109 NAL Call. No.: QK710.P68 Molecular characterization and expression of alfalfa isoliquiritigenin 2'-O-methyltransferase, an enzyme specifically involved in the biosynthesis of an inducer of Rhizobium meliloti nodulation genes. Maxwell, C.A.; Harrison, M.J.; Dixon, R.A. 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. 971-981; 1993 Dec. Includes references.

Language: English

Descriptors: Medicago sativa; Nodulation; Roots; Transcription; Amino acid sequences; Gene expression; Genetic code; Molecular biology; Nucleotide sequences; Protein synthesis; Rhizobium meliloti

110 NAL Call. No.: QK710.P62 Molecular characterization and expression of an isocitrate dehydrogenase from alfalfa (Medicago sativa L.).
Shorrosh, B.S.; Dixon, R.A.
Dordrecht : Kluwer Academic Publishers; 1992 Dec. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 20 (5): p. 801-808; 1992 Dec. Includes references.

Language: English

Descriptors: Medicago sativa; Structural genes; Isocitrate dehydrogenase; Dna; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Multigene families; Plant development

Abstract: A putative isocitrate dehydrogenase (IDH) cDNA from alfalfa has been cloned and sequenced. The derived amino acid sequence of 433 residues contains the isocitrate and isopropylmalate dehydrogenase signatures, is 63% identical to yeast mitochondrial NADP-IDH and shares high sequence identity with peptides of pig heart NADP-IDH. The sequence contains a potential N-terminal leader with similarities to a thylakoid transit peptide. IDH transcripts and NADP-IDH activity were detected in all alfalfa tissues examined, their levels depending upon the tissue type and its developmental stage. Transcripts and enzymatic activity were not induced on exposure of cell suspension cultures to a fungal elicitor. IDH is encoded by a small gene family in alfalfa.

111 NAL Call. No.: QK710.P62 Molecular characterization of a pea beta-1,3-glucanase induced by Fusarium solani and chitosan challenge.
Chang, M.M.; Hadwiger, L.A.; Horovitz, D. Dordrecht : Kluwer Academic Publishers; 1992 Nov. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 20 (4): p. 609-618; 1992 Nov. Includes references.

Language: English

Descriptors: Pisum sativum; Fusarium solani f.sp. phaseoli; Fusarium solani f.sp. pisi; Structural genes; Beta-glucanase; Dna; Nucleotide sequences; Amino acid sequences; Disease resistance; Defense mechanisms; Fungal diseases; Chitosan; Gene expression; Messenger RNA; Stems; Roots; Pods; Genetic regulation

Abstract: beta-glucanases are prominent proteins in pea endocarp tissue responding to fungal infection. We have cloned and sequenced a partial pea cDNA clone, pPIG312, corresponding to a beta-1,3-glucanase in pea pods challenged with the incompatible pathogen Fusarium solani f. sp. phaseoli. The insert from the partial pea cDNA was used to probe a genomic library derived from pea leaves of the same cultivar. One of the genomic clones, pPIG4-3, contained the complete coding sequence for a mature beta-1,3-glucanase protein. The predicted amino acid sequence of the pea beta-1,3-glucanase has 78% identity to bean beta-1,3-glucanase, 62% and 60% to two tobacco beta-1,3-glucanases, 57% to soybean beta-1,3-glucanase, 51% to barley beta-1,3-glucanase, and 48% to barley beta-1,3-1,4-glucanase. Genomic Southern analysis indicates that the pea genome contains only one beta-1,3-glucanase gene corresponding to the probe used in this study. Accumulation of beta-1,3-glucanase mRNA homologous with the pPIG312 probe was detected in pea pods within 4 to 8 h after challenge with F. solani f. sp. phaseoli, f. sp. pisi, a compatible strain, or the elicitor, chitosan. In the incompatible reaction, mRNA accumulation remained high for 48h, whereas it rapidly decreased in the compatible reaction. After fungal inoculation of whole pea seedlings, the enhanced mRNA accumulation occurred mainly in the basal region (lower stem and root). This beta-1,3-glucanase mRNA was constitutively expressed in the roots of pea seedlings. The sustained levels of beta-glucanase mRNA expression induced by the incompatible pathogen in the resistance response suggests that the enzyme contributes to the pea plant's general defense.

112 NAL Call. No.: 450 P699 Molecular characterization of a rapidly and transiently wound-induced soybean (Glycine max L.) gene encoding 1-aminocyclopropane-1-carboxylate synthase. Liu, D.; Li, N.; Dube, S.; Kalinski, A.; Herman, E.; Mattoo, A.K. Kyoto, Japan : Japanese Society of Plant Physiologists; 1993 Oct. Plant and cell physiology v. 34 (7): p. 1151-1157; 1993 Oct. Includes references.

Language: English

Descriptors: Glycine max; Lyases; Acc; Auxins; Ethylene; Gene expression; Genetic code; Healing; Molecular genetics; Amino acid sequences; Nucleotide sequences

Abstract: A complementary DNA clone, designated GMACS1, encoding an mRNA for soybean 1-aminocyclopropane-1-carboxylate (ACC) synthase was isolated from a leaf cDNA library, and its nucleotide sequence was determined. The GMACS1-specific transcript was found to rapidly but transiently accumulate upon wounding in soybean leaf, pod and seed, and was not induced by 2,4-D, or by ethylene. However, the transcript level increased 37-fold in the presence of cycloheximide.

113 NAL Call. No.: QK725.P532 Molecular characterization of NADH-dependent glutamate synthase from alfalfa nodules.
Gregerson, R.G.; Miller, S.S.; Twary, S.N.; Gantt, J.S.; Vance, C.P. Rockville, Md. : American Society of Plant Physiologists; 1992 Feb. The Plant cell v. 5 (2): p. 215-226; 1992 Feb. Includes references.

Language: English

Descriptors: Medicago sativa; Glutamate-ammonia ligase; Nadh; Complementary DNA; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Genetic regulation; Nitrogen fixation; Bacteroids; Root nodules; Rhizobium meliloti; Enzyme activity

Abstract: Alfalfa NADH-dependent glutamate synthase (NADH-GOGAT), together with glutamine synthetase, plays a central role in the assimilation of symbiotically fixed nitrogen into amino acids in root nodules. Antibodies previously raised against purified NADH-GOGAT were employed to screen a cDNA library prepared using RNA isolated from nodules of 20-day-old alfalfa plants. A 7.2-kb cDNA clone was obtained that contained the entire protein coding region of NADH-GOGAT. Analysis of this cDNA and determination of the amino-terminal amino acids of the purified protein revealed that NADH-GOGAT is synthesized as a 2194-amino acid protein that includes a 101-amino acid presequence. The deduced amino acid sequence shares significant identity with maize ferredoxin-dependent GOGAT, and with both large and small subunits of Escherichia coli NADPH-GOGAT. DNA gel blot analysis of alfalfa genomic DNA suggests the presence of a single NADH-GOGAT gene or a small gene family. The expression of NADH-GOGAT mRNA, enzyme protein, and enzyme activity was developmentally regulated in root nodules. A dramatic increase in gene expression occurred coincidentally with the onset of nitrogen fixation in the bacteroid, and was absent in both ineffective plants that were nodulated with effective Rhizobium meliloti and effective plants that had been nodulated with ineffective R. meliloti strains. Maximum NADH-GOGAT expression, therefore, appears to require an effective, nitrogen-fixing symbiosis.

114 NAL Call. No.: 450 P692 Molecular cloning and evidence for osmoregulation of the delta1-pyrroline-5-carboxylate reductase (proC) gene in pea (Pisum sativum L.).
Williamson, C.L.; Slocum, R.D.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov. Plant physiology v. 100 (3): p. 1464-1470; 1992 Nov. Includes references.

Language: English

Descriptors: Pisum sativum; Complementary DNA; Structural genes; Oxidoreductases; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Genetic regulation; Osmotic pressure; Osmoregulation; Roots; Leaves; Seedlings; Greening; Salinity; Sodium chloride

Abstract: Several cDNA clones encoding delta 1-pyrroline-5-carboxylate reductase (P5CR, L-proline:NAD[P]+ 5-oxidoreductase, EC 1.5.1.2), which catalyzes the terminal step in proline biosynthesis, were isolated from a pea leaf library screened with a 32P-labeled Aval fragment of a soybean nodule P5CR cDNA (A.J. Delauney, D.P.S. Verma [1990) Mol Gen Genet 221: 299-305). DNA sequence analysis of one full-length 1.3-kb clone (PPPS3) indicated that the pea P5CR gene contains a single major open reading frame encoding a polypeptide of 28,242 Da. Genomic analysis suggested that two to three copies of the P5CR gene are present per haploid genome in pea. The primary structure of pea P5CR is 85% identical with that of soybean and exhibits significant homology to human, yeast, and Escherichia coli P5CR. The sequence of one of four highly conserved domains found in all prokaryotic and eukaryotic P5CRS is similar to the consensus sequence for the NAD(P)H-binding site of other enzymes. The pea P5CR cDNA hybridized to two transcripts, 1.3 and 1.1 kb in size, in polyadenylated RNA purified from leaf tissues of mature, light-grown plants (4 weeks old). Only the 1.3-kb transcript was detected in younger (1 week old) greened seedlings or in etiolated seedlings. In greened seedlings, steady-state levels of this 1.3-kb mRNA increased approximately 5-fold in root tissues within 6 h after plants were irrigated with 0.4 m NaCl, suggesting that expression of the P5CR gene is osmoregulated.

115 NAL Call. No.: 450 P692 Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an enzyme involved in the resistance response of soybean (Glycine max L.) against pathogen attack.
Uhlmann, A.; Ebel, J.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug. Plant physiology v. 102 (4): p. 1147-1156; 1993 Aug. Includes references.

Language: English

Descriptors: Glycine max; Complementary DNA; Ligases; Isoenzymes; Nucleotide sequences; Amino acid sequences; Multigene families; Messenger RNA; Gene expression; Genetic regulation; Beta-glucan; Cell wall components; Phytophthora megasperma; Defense mechanisms

Abstract: We have isolated three classes of cDNAs that probably encode three 4-coumarate:coenzyme A ligase (4CL) isoenzymes in soybean (Glycine max L.). The deduced amino acid sequences reveal several regions of extended sequence identity among 4CLs of all plants analyzed to date. The sequences of two of these regions are consistent with a domain structure proposed for a group of enzymes catalyzing the ATP-dependent covalent binding of AMP to their substrates during the reaction sequence. By using two cDNA fragments that do not cross-hybridize under the conditions used, we demonstrate that 4CL in soybean is very likely encoded by a small gene family. Members of this family are differentially expressed in soybean cell cultures treated with beta-glucan elicitors of Phytophthora megasperma f. sp. glycinea or in soybean roots infected with either an incompatible or compatible race of the fungus. These results are in agreement with our previous observation that elicitor treatment of soybean cells caused a preferential enhancement in the activity level of one of the 4CL isoenzymes. In soybean, 4CL isoenzymes possessing different substrate affinities for substituted cinnamic acids, and showing differential regulation to environmental stress, may play a pivotal role in distributing substituted cinnamate intermediates at a branch point of general phenylpropanoid metabolism into subsequent specific pathways.

116 NAL Call. No.: QH431.G452 Molecular cloning and expression of a cDNA encoding the proliferating cell nuclear antigen from Brassica napus (oilseed rape). Markley, N.A.; Bonham-Smith, P.C.; Moloney, M.M. Ottawa, Ontario, Canada : National Research Counci l Canada; 1993 Jun. Genome / v. 36 (3): p. 459-466; 1993 Jun.

Language: English

Descriptors: Brassica napus; Complementary DNA; Plant proteins; Antigens; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Immunochemistry; Dna replication; Dna polymerase

Abstract: A cDNA clone encoding the proliferating cell nuclear antigen (PCNA) has been isolated from a Brassica napus apical meristem cDNA library. The putative full-length cDNA contains an open reading frame of 1004 nucleotides, which predicts a protein of 263 amino acids (Mr = 29 231). Sequence analysis has revealed that the plant PCNA exhibits 81.6% amino acid similarity with the human PCNA. Genomic Southern blot analysis indicates the presence of at least two copies of PCNA per genome. The B. napus PCNA mRNA (1.0 kb) was expressed in rapidly dividing tissues such as flower buds, apical meristems, and young leaves, while mature stem and fully expanded leaves showed significantly lower levels of PCNA transcript. The B. napus PCNA cDNA was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase (GST) in the bacterial expression vector pGEX-2T. A broad specificity monoclonal antibody raised against rabbit PCNA cross-reacted with the GST-PCNA fusion peptide but not with the GST moiety alone. This antibody also recognized the human PCNA (36 kDa) polypeptide, confirming the structural similarities between the human and plant PCNA. The high degree of structural conservation of PCNA from such diverse organisms as humans and higher plants suggests that the plant PCNA may function in a manner analogous to that found in mammals with respect to plant cell DNA replication. Such conservation suggests that PCNA is also a critical component of the plant cell DNA replication complex.

117 NAL Call. No.: QK710.P62 Molecular cloning and sequencing analysis of a beta-tubulin gene from Lupinus albus.
Vassilevskaia, T.D.; Ricardo, C.P.; Rodrigues-Pousada, C. Dordrecht : Kluwer Academic Publishers; 1993 Jul. Plant molecular biology v. 22 (4): p. 716-718; 1993 Jul. Includes references.

Language: English

Descriptors: Lupinus albus; Structural genes; Complementary DNA; Tubulin; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Roots; Leaves; Flowers; Multigene families

Abstract: Genomic lambda-dash library constructed from Lupinus albus nuclear DNA was screened using a fragment of the beta-tubulin cDNA (beta 8-31) clone of Chlamydomonas reinhardtii as probe. One of the positive recombinant phages was isolated, subcloned and analysed by sequencing. We present here nucleotide and derived amino acid sequences of the beta-tubulin gene, designated as L beta 1 and identified by similarity with other beta-tubulins. The L beta 1-encoded protein reveals a very high degree of similarity with other plant tubulins and contains consensus sequences for binding guanine base, phosphate and Mg2+. Northern analysis of total RNA isolated from roots, leaves, flowers and pools revealed that Lupinus albus beta-tubulin genes are constitutively expressed in all studied plant tissues.

118 NAL Call. No.: 450 P692 Molecular cloning of abscisic acid-responsive mRNAs expressed during the induction of freezing tolerance in bromegrass (Bromus inermis Leyss) suspension culture.
Lee, S.P.; Chen, T.H.H.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Mar. Plant physiology v. 101 (3): p. 1089-1096; 1993 Mar. Includes references.

Language: English

Descriptors: Bromus inermis; Messenger RNA; Plant proteins; Alcohol oxidoreductases; Cloning; Complementary DNA; Gene expression; Genetic regulation; Abscisic acid; Freezing; Tolerance; Cell suspensions; Nucleotide sequences; Amino acid sequences; Cold; Acclimatization

Abstract: Abscisic acid (ABA) increases the freezing tolerance of bromegrass (Bromus inermis Leyss) cell-suspension cultures at 23 degrees C and elicits many metabolic changes similar to those observed during cold acclimation. Induction and maintenance of freezing tolerance by ABA is accompanied by the expression of novel polypeptides and translatable RNAs. The objective of this study was to isolate and characterize ABA-responsive cDNAs associated with ABA-induced freezing tolerance in bromegrass cell cultures. Among the 16 ABA-responsive cDNA clones isolated, 9 were expressed only with ABA treatment, 7 showed increased transcript level, and 1 was transiently expressed. Cold responsiveness was determined in three clones with increased transcript levels and in the transiently expressed clone. Deacclimation of ABA-hardened cells was a relatively slow process, because all of the novel transcripts persisted for at least 7 d after cells were cultured in ABA-free medium. Preliminary sequencing of cDNAs has identified several clones that share high sequence homology with genes associated with sugar metabolism, osmotic stress, and protease activity. Clone pBGA61 was fully sequenced and tentatively identified as an NADPH-dependent aldose reductase. The predicted amino acid sequence of the coding region shared 92% similarity with that predicted for barley aldose reductase cDNA. It is proposed that expression of genes related to sugar metabolism and osmotic stress may be required for ABA-induced hardening.

119 NAL Call. No.: QK710.P68 The MsK family of alfalfa protein kinase genes encodes homologues of shaggy/glycogen synthase kinase-3 and shows differential expression patterns in plant organs and development.
Pay, A.; Jonak, C.; Bogre, L.; Meskiene, I.; Mairinger, T.; Szalay, A.; Heberle-Bors, E.; Hirt, H.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993 Jun.
The plant journal v. 3 (6): p. 847-856; 1993 Jun. Includes references.

Language: English

Descriptors: Medicago sativa; Structural genes; Multigene families; Protein kinase; Nucleotide sequences; Amino acid sequences; Complementary DNA; Gene expression; Messenger RNA; Cell suspensions; Leaves; Petioles; Stems; Roots; Flowering; Plant embryos

120 NAL Call. No.: QK710.P68 Multiple functions of promoter sequences involved in organ-specific expression and ammonia regulation of a cytosolic soybean glutamine synthetase gene in transgenic Lotus corniculatus.
Marsolier, M.C.; Carrayol, E.; Hirel, B. Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993 Mar.
The plant journal v. 3 (3): p. 405-414; 1993 Mar. Includes references.

Language: English

Descriptors: Lotus corniculatus; Glycine max; Genes; Promoters; Gene expression; Gene transfer; Transgenics; Glutamate-ammonia ligase; Enzyme activity; Regulation; Ammonia; Histochemistry; Plant morphology; Plant anatomy

121 NAL Call. No.: QK725.P532 A mutant lectin gene is rescued from an insertion element that blocks its expression.
Okamuro, J.K.; Goldberg, R.B.
Rockville, Md. : American Society of Plant Physiologists; 1992 Sep. The Plant cell v. 4 (9): p. 1141-1146; 1992 Sep. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Structural genes; Lectins; Alleles; Mutations; Genetic regulation; Gene expression; Transcription; Controlling elements; Genetic transformation; Transgenics; Promoters; Embryogenesis

Abstract: The soybean lectin gene Le1 encodes a prevalent seed protein and is highly regulated during the life cycle. The mutant lectin gene allele le1 is not transcribed detectably, contains a 3.5-kb Tgm1 insertion element within its coding region 0.6 kb 3' to the transcription start site, and leads to a lectinless phenotype. To determine whether the Tgm1 element or a secondary mutation was responsible for repressing le1 gene transcription, we eliminated the insertion element by constructing a chimeric lectin gene (le1/Le1) that contained the 5' half of the le1 gene and its promoter region and the 3' half of the wild-type Le1 gene. Transformed tobacco seed containing the le1/Le1 gene produced both lectin mRNA and protein, demonstrating that the mutant lectin gene control region is transcriptionally competent. By contrast, transformed seed containing the le1 gene produced no detectable lectin mRNA. We conclude that the absence of detectable transcription from the le1 gene is due to transcriptional inhibition by the Tgm1 insertion element and that this element acts at a distance to block transcription from an upstream promoter region.

122 NAL Call. No.: 450 J8224 A mutation in Vicia faba results in ineffective nodules with impaired bacteroid differentiation and reduced synthesis of late nodulins. Haser, A.; Robinson, D.L.; Duc, G.; Vance, C.P. Oxford : Oxford University Press; 1992 Nov. Journal of experimental botany v. 43 (256): p. 1397-1407; 1992 Nov. Includes references.

Language: English

Descriptors: Vicia faba; Rhizobium; Root nodules; Nodulation; Bacteroids; Cell differentiation; Mutants; Recessive genes; Mutations; Nodulins; Protein synthesis; Nitrogen fixation; Acetylene reduction; Enzymes; Enzyme activity; Gene expression; Messenger RNA

Abstract: Although numerous reports have documented the effect of bacterially-induced ineffectiveness on root nodule structure, function, and plant gene expression, few studies have detailed the effect of the plant genome on similar parameters. In this report effective (N2-fixing) broadbean (Vicia faba L.) and plant-controlled ineffective (non-N2-fixing) broadbean recessive for the sym-1 gene were compared for nodule structure, developmental expression of nodule enzyme activities, enzyme proteins, and mRNAs involved in N assimilation, leghemoglobin (Lb) synthesis, and acetylene reduction activity (ARA). During development of effective wild-type nodules, glutamine synthetase (GS), aspartate aminotransferase (AAT), phosphoenolpyruvate carboxylase (PEPC) and NADH-glutamate synthase (GOGAT) activities and enzyme proteins increased coincident with nodule ARA. The increases in GS, AAT, and PEPC were associated with increased synthesis of mRNAs for these proteins. Synthesis of Lb polypeptides and mRNAs during development of effective nodules was similar to that of GS, AAT, and PEPC. By contrast, ineffective sym-1 nodules displayed little or no ARA and had neither the increases in enzyme activities nor enzyme proteins and mRNAs as seen for effective nodules. The effect of the sym-1 gene appeared to occur late in nodule development at either the stage of bacterial release from infection threads or differentiation of bacteria into bacteroids. High in vitro enzyme activities, enzyme polypeptides, and mRNA levels in parental effective nodules were dependent upon a signal associated with effective bacteroids that was lacking in sym-1 nodules. Nodule organogenesis did not appear to be a signal for the induction of GS, PEPC, AAT, and Lb expression in sym-1 nodules.

123 NAL Call. No.: 442.8 Z8 NADP+ glyceraldehyde-3-phosphate dehydrogenase in soybeans [glycine max (L.) Merr.]: genetics and developmental expression. Delorme, R.M.; Skorupska, H.T.
Berlin, W. Ger. : Springer International; 1993 Feb. Theoretical and applied genetics v. 85 (6/7): p. 851-856; 1993 Feb. Includes references.

Language: English

Descriptors: Glycine max; Inheritance; Loci; Alleles; Genetic variation; Glyceraldehyde-3-phosphate dehydrogenase; Nadp; Electrophoresis; Enzyme polymorphism; Gene expression; Plant development; Linkage; Linkage groups; Cultivars; Pedigree; Line differences; Lines; Chloroplasts; Genetic change

Abstract: Chloroplastic (NADP+) glyceraldehyde-3-phosphate dehydrogenase (E.C. 1.2.1.9) catalyzes the second reaction in photosynthesis after the fixation of carbon by Rubisco. Chloroplast-bound (NADP+) G3PDH was resolved in soybean by starch gel electrophoresis using L-histidine-citrate buffer (pH 5.7). Histochemical staining revealed zymogram patterns indicative of a tetramer. A survey of soybean genotypes revealed differences in zymogram patterns between the principal cytoplasmic sources of the northern and southern US germplasms. In the soybean pedigree, an allelic frequency shift toward a five-banded pattern was observed. G3PDH polymorphism was due to allele associated with gene expression at the slow locus. No linkage was found between the slow locus of (NADP+) G3PDH and ACO2, ACO3, ACO4, ACP, DIA1, IDH1, IDH2, PGM1, and PGM3. Developmental expression in the above-ground tissues was identical, whereas roots as a rule did not express (NADP+) G3PDH activity. The importance of chloroplast-bound (NADP+) G3PDH in photo-synthesis and its interesting mode of inheritance warrants further exploration of this enzyme in soybean.

124 NAL Call. No.: 450 P692 New cold- and drought-regulated gene from Medicago sativa. Laberge, S.; Castonguay, Y.; Vezina, L.P. Rockville, Md. : American Society of Plant Physiologists; 1993 Apr. Plant physiology v. 101 (4): p. 1411-1412; 1993 Apr. Includes references.

Language: English

Descriptors: Medicago sativa; Complementary DNA; Multigene families; Plant proteins; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Genetic regulation; Cold stress; Water stress; Drought; Acclimatization

125 NAL Call. No.: 450 P692 A new cold-induced alfalfa gene is associated with enhanced hardening at subzero temperature.
Monroy, A.F.; Castonguay, Y.; Laberge, S.; Sarhan, F.; Vezina, L.P.; Dhindsa, R.S.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul. Plant physiology v. 102(3): p. 873-879; 1993 Jul. Includes references.

Language: English

Descriptors: Medicago sativa; Complementary DNA; Structural genes; Plant proteins; Nucleotide sequences; Amino acid sequences; Cold hardening; Freezing; Tolerance; Gene expression; Messenger RNA; Genetic regulation; Cold

Abstract: When alfalfa (Medicago sativa L. cv Apica) plants grown at room temperature are transferred to 2 degrees C, the temperature at which 50% of the plants fail to survive (LT50) decreases from -6 to -14 degrees C during the first 2 weeks but then increases to 9 degrees C during the subsequent 2 weeks. However, when plants are kept for 2 weeks at 2 degrees C and then transferred to 2 degrees C for another two weeks, the LT50 declines to 16 degrees C. These changes in freezing tolerance are paralleled by changes in transcript levels of cas15 (cold acclimation-specific gene encoding a 14.5-kD protein), a cold-induced gene. Cold-activation of cas15 occurs even when protein synthesis is inhibited by more than 90%, suggesting that cold-initiated events up to and including the accumulation of cas15 transcripts depend on preexisting gene products. cas15 shows little homology to any known gene at the nucleotide or amino acid level. The deduced polypeptide (CAS15) of 14.5 kD contains four repeats of a decapeptide motif and possesses a bipartite sequence domain at the carboxy terminus with homology to the reported nuclear-targeting signal sequences. Although the relative amount of cas15 DNA as a fraction of the total genomic DNA is similar in cultivars with different degrees of freezing tolerance, its organization in the genome is different. The possible role of cas15 in the development of cold-induced freezing tolerance is discussed.

126 NAL Call. No.: QK710.A9 Nodulation and nodulin gene expression in an interspecific hybrid between Glycine max and Glycine tomentella.
Shen, B.; Davis, L.C.
East Melbourne : Commonwealth Scientific and Industrial Research Organization; 1992.
Australian journal of plant physiology v. 19 (6): p. 693-707; 1992. Includes references.

Language: English

Descriptors: Glycine tomentella; Glycine max; Interspecific hybridization; Gene expression; Hybrids; Nodulins; Nodulation; Nitrogen fixation; Rhizobium fredii; Bradyrhizobium japonicum

127 NAL Call. No.: SB732.6.M65 Pathological and molecular characterizations of alfalfa interactions with compatible and incompatible bacteria, Xanthomonas campestris pv. alfalfae and Pseudomonas syringae pv. pisi.
Esnault, R.; Buffard, D.; Breda, C.; Sallaud, C.; El Turk, J.; Kondorosi, A. St. Paul, MN : APS Press, [c1987-; 1993 Sep. Molecular plant-microbe interactions : MPMI v. 6 (5): p. 655-664; 1993 Sep. Includes references.

Language: English

Descriptors: Medicago sativa; Xanthomonas campestris pv. alfalfae; Pseudomonas syringae pv. pisi; Disease resistance; Defense mechanisms; Gene expression; Messenger RNA; Oxidoreductases; Chalcone isomerase; Naringenin-chalcone synthase; Roots; Leaves; Pathogenesis-related proteins; Nucleotide sequences; Amino acid sequences; Complementary DNA

128 NAL Call. No.: QK725.P532 Patterns of soybean proline-rich protein gene expression. Wyatt, R.E.; Nagao, R.T.; Key, J.L.
Rockville, Md. : American Society of Plant Physiologists; 1992 Jan. The Plant cell v. 4 (1): p. 99-100; 1992 Jan. Includes references.

Language: English

Descriptors: Glycine max; Multigene families; Plant proteins; Proline; Gene expression; Messenger RNA; Cell wall components; Hypocotyls; Xylem; Phloem; Testas; Seeds; Epidermis; Leaves; Cotyledons

Abstract: The expression patterns of three members of a gene family that encodes proline-rich proteins in soybean (SbPRPs) were examined using in situ hybridization experiments. In most instances, the expression of SbPRP genes was intense in a limited number of cell types of a particular organ. SbPRP1 RNA was localized in several cell types of soybean hypocotyls, including cells within the phloem and xylem. SbPRP1 expression increased within epidermal cells in the elongating and mature regions of the hypocotyl; expression was detected also in lignified cells surrounding the hilum of mature seeds. SbPRP2 RNA was present in cortical cells and in the vascular tissue of the hypocotyl, especially cells of the phloem. This gene was expressed also in the inner integuments of the mature seed coat. SbPRP3 RNA was localized specifically to the endodermoid layer of cells surrounding the stele in the elongating region of the hypocotyl, as well as in the epidermal cells of leaves and cotyledons. These data show that members of this gene family exhibit cell-specific expression. The members of the SbPRP gene family are expressed in different types of cells and in some cell types that also express the glycine-rich protein or hydroxyproline-rich glycoprotein classes of genes.

129 NAL Call. No.: QK710.P68 The plant homologue of MAP kinase is expressed in a cell cycle-dependent and organ-specific manner.
Jonak, C.; Pay, A.; Bogre, L.; Hirt, H.; Heberle-Bors, E. Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993 Apr.
The plant journal v. 3 (4): p. 611-617; 1993 Apr. Includes references.

Language: English

Descriptors: Medicago sativa; Medicago varia; Clones; Genetic analysis; Nucleotide sequences; Amino acid sequences; Genetic code; Dna; Kinases; Microtubules; Plant proteins; Gene expression; Transcription

130 NAL Call. No.: QK725.P532 Pollen-stigma signaling in the sporophytic self-incompatibility response. Nasrallah, J.B.; Nasrallah, M.E.
Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Oct. The Plant cell v. 5 (10): p. 1325-1335; 1993 Oct. In the special issue: Special review issue on plant reproduction. Includes references.

Language: English

Descriptors: Brassica campestris; Brassica napus; Brassica oleracea; Self incompatibility; Pollen; Stigma; Pollen tubes; Loci; Multigene families; Glycoproteins; Protein kinase; Gene expression; Literature reviews

131 NAL Call. No.: QK710.P68 Prediction of germ-line transformation events in chimeric R0 transgenic soybean plantlets using tissue-specific expression patterns. Christou, P.; McCabe, D.E.
Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers in association with the Society for Experimental Biology, c1991-; 1992 May. The Plant journal : for cell and molecular biology v. 2 (3): p. 283-290; 1992 May. Includes references.

Language: English

Descriptors: Glycine max; Genetic transformation; Germ line; Chimeras; Transgenic plants; Gene expression; Genetic markers; Beta-glucuronidase; Enzyme activity; Genetic improvement; Phenotypes; Developmental stages; Plant anatomy; Plant morphology

132 NAL Call. No.: 450 P692 Proteolysis during development and senescence of effective and plant gene-controlled ineffective alfalfa nodules. Pladys, D.; Vance, C.P.
Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Oct. Plant physiology v. 103 (2): p. 379-384; 1993 Oct. Includes references.

Language: English

Descriptors: Medicago sativa; Root nodules; Plant composition; Nodulins; Senescence; Genetic regulation; Proteolysis; Cysteine; Proteinases; Enzyme activity; Ph; Genotypes; Genetic variation; Plant development; Protein composition; Symbiosis; Gene expression; Phosphoenolpyruvate carboxylase; Leghemoglobin

Abstract: Plant-controlled ineffective root nodules, conditioned by the in1 gene in medicago sativa L. cv Saranac, undergo premature senescence and have reduced levels of many late nodulins. To ascertain which factors contribute to premature senescence, we have evaluated proteolysis as it occurs throughout the development of ineffective Saranac (in1Sa) and effective Saranac nodules. Cysteine protease activities with acidic pH optimum and enzyme proteins were present in both genotypes. We found that acidic protease activity was low in effective Saranac nodules throughout their development. In contrast, by 2 weeks after inoculation, acid protease activity of in1Sa nodules was severalfold higher than that of Saranac nodules and remained high until the experiment was terminated 8 weeks later. This increase in protease enzyme activity correlated with an increase in protease protein amounts. Increased protease activity and amount in in1Sa nodules was correlated with a decrease in nodule soluble protein. The time at which in1Sa nodules initially showed increased protease activity corresponded to when symbiosis deteriorated. High levels of phosphoenolpyruvate carboxylase (PEPC) protein were expressed in effective nodules by 12 d after inoculation and expression was associated with low proteolytic enzyme activity. In contrast, although PEPC was expressed in in1Sa nodules, PEPC protein was not found 12 d after inoculation and thereafter. Acidic protease from in1Sa nodules could also degrade purified leghemoglobin. These data indicate that premature senescence and low levels of late nodulins in in1Sa nodules can be correlated in part with increased proteolysis.

133 NAL Call. No.: SB732.6.M65 pSym nod gene influence on elicitation of peroxidase activity from white clover and pea roots by rhizobia and their cell-free supernatants. Salzwedel, J.L.; Dazzo, F.B.
St. Paul, Minn. : APS Press; 1993 Jan.
Molecular plant-microbe interactions : MPMI v. 6 (1): p. 127-134; 1993 Jan. Includes references.

Language: English

Descriptors: Trifolium repens; Pisum sativum; Rhizobium trifolii; Rhizobium leguminosarum; Peroxidase; Enzyme activity; Roots; Root hairs; Gene expression; Plasmids; Plant; Nodulation; Peroxidases

134 NAL Call. No.: 450 P692 Regenertion of transgenic soybean (Glycine Max) plants from electroporated protoplasts.
Dhir, S.K.; Dhir, S.; Savka, M.A.; Belanger, F.; Kriz, A.L.; Farrand, S.K.; Widholm, J.M.
Rockville, Md. : American Society of Plant Physiologists; 1992 May. Plant physiology v. 99 (1): p. 81-88; 1992 May. Includes references.

Language: English

Descriptors: Glycine max; Transgenics; Protoplasts; Callus; Regenerative ability; Genetic transformation; Gene transfer; Gene expression

Abstract: Transgenic soybean (Glycine max [L.] Merr.) plants were regenerated from calli derived from protoplasts electroporated with plasmid DNA-carrying genes for a selectable marker, neomycin phosphotransferase (NPTII), under the control of the cauliflower mosaic virus 35-Svedberg unit promoter, linked with a nonselectable mannityl opine synthesis marker. Following electroporation and culture, the protoplast-derived colonies were subjected to kanamycin selection (50 micrograms per milliliter) beginning on day 15 for 6 weeks. Approximately, 370 to 460 resistant colonies were recovered from 1 X 10(6) electroporated protoplasts, giving an absolute transformation frequency of 3.7 to 4.6 X 10(-4). More than 80% of the kanamycin-resistant colonies showed NPTII activity, and about 90% of these also synthesized opines. This indicates that the linked marker genes were co-introduced and co-expressed at a very high frequency. Plants were regenerated from the transformed cell lines. Southern blot analysis of the transformed callus and leaf DNA demonstrated the integration of both genes. Single-plant assays performed with different plant parts showed that both shoot and root tissues express NPTII activity and accumulate opines. Experiments with NPTII and mannityl opine synthesis marker genes on separate plasmids resulted in a co-expression rate of 66%. These results indicate that electroporation can be used to introduce both linked and unlinked genes into the soybean to produce transformed plants.

135 NAL Call. No.: QK710.P62 Regulatable endogenous production of cytokinins up to 'toxic' levels in transgenic plants and plant tissues.
Ainley, W.M.; McNeil, K.J.; Hill, J.W.; Lingle, W.L.; Simpson, R.B.; Brenner, M.L.; Nagao, R.T.; Key, J.L.
Dordrecht : Kluwer Academic Publishers; 1993 Apr. Plant molecular biology v. 22 (1): p. 13-23; 1993 Apr. Includes references.

Language: English

Descriptors: Glycine max; Nicotiana tabacum; Agrobacterium tumefaciens; Gene expression; Structural genes; Acyltransferases; Isopentenyladenosine; Recombinant DNA; Promoters; Heat shock proteins; Genetic regulation; Heat shock; Transgenic plants; Genetic transformation; Shoots; Organogenesis

Abstract: The effects of expressing a chimeric gene consisting of a soybean heat shock gene promoter and a sequence that encodes an enzyme catalyzing the synthesis of a potent phytohormone, the cytokinin iPMP, have been analyzed in transgenic tobacco plants. The production of cytokinin endogenously produced several effects previously undocumented. The differentiation of shoots independent of exogenous cytokinin from heat-treated transgenic plant leaf explants demonstrates that long-term heat treatments do not interfere with complex developmental processes. This extends the potential usefulness of heat shock gene promoters to conditionally express genes during windows of development that span several weeks.

136 NAL Call. No.: 450 P692 Regulation of expression of proteinase inhibitor genes by methyl jasmonate and jasmonic acid.
Farmer, E.E.; Johnson, R.R.; Ryan, C.A. Rockville, Md. : American Society of Plant Physiologists; 1992 Mar. Plant physiology v. 98 (3): p. 995-1002; 1992 Mar. Includes references.

Language: English

Descriptors: Lycopersicon esculentum; Medicago sativa; Nicotiana tabacum; Proteinases; Enzyme inhibitors; Protein synthesis; Gene expression; Regulation; Jasmonic acid; Derivatives; Messenger RNA; Induction

Abstract: Gel electrophoretic analysis of the proteinase inhibitor proteins induced in tomato leaves by airborne methyl jasmonate (EE Farmer, CA Ryan [1990] Proc Natl Acad Sci USA 87: 7713-7716) revealed the new appearance of inhibitors I and II and two other, higher molecular mass proteins (63.5 and 87 kilodaltons). Northern analysis of methyl jasmonate-induced inhibitors I and II mRNAs in tomato (Lycopersicon esculentum) leaves, and of alfalfa trypsin inhibitor (a Bowman-Birk family inhibitor) mRNA in alfalfa (Medicago sativa) leaves, indicated that nascent inhibitor mRNAs were regulated in a manner similar to wounding, that is, at the transcriptional level. In tobacco (Nicotiana tabacum), transformed with a fused gene composed of the 5' and 3' regions of a wound-inducible potato inhibitor II and a chloramphenicol acetyl transferase (CAT) gene coding region, CAT activity was induced in leaves by methyl jasmonate, consistent with a transcriptional regulation of the inhibitor II gene. In tomato leaves, inhibitor I and II mRNAs and proteins accumulated in leaves distal to those exposed to methyl jasmonate or jasmonic acid to similar levels as in exposed leaves. We suggest that in response to wound signals generated by insect or pathogen attacks, linolenic acid is released into the cytoplasm from plant cell membrane lipids and is rapidly converted in cells to jasmonic acid (or perhaps a closely related derivative such as methyl jasmonate), which serves as a signal to regulate the expression of proteinase inhibitor genes.

137 NAL Call. No.: QK725.P532 Rhizobium meliloti elicits transient expression of the early nodulin gene ENOD12 in the differentiating root epidermis of transgenic alfalfa. Pichon, M.; Journet, E.P.; Dedieu, A.; Billy, F. de; Truchet, G.; Barker, D.G. Rockville, Md. : American Society of Plant Physiologists; 1992 Oct. The Plant cell v. 4 (10): p. 1199-1211; 1992 Oct. Includes references.

Language: English

Descriptors: Medicago truncatula; Rhizobium meliloti; Gene expression; Structural genes; Nodulins; Nodulation; Roots; Epidermis; Root nodules; Transgenics; Genetic transformation; Transcription; Genetic regulation; Nucleotide sequences; Amino acid sequences; Restriction mapping

Abstract: To study the molecular responses of the host legume during early stages of the symbiotic interaction with Rhizobium, we have cloned and characterized the infection-related early nodulin gene MtENOD12 from Medicago truncatula. in situ hybridization experiments have shown that, within the indeterminate Medicago nodule, transcription of the MtENOD12 gene begins in cell layers of meristematic origin that lie ahead of the infection zone, suggesting that these cells are undergoing preparation for bacterial infection. Histochemical analysis of transgenic alfalfa plants that express an MtENOD12 promoter-beta-glucuronidase gene fusion has confirmed this result and further revealed that MtENOD12 gene transcription occurs as early as 3 to 6 hr following inoculation with R. meliloti in a zone of differentiating root epidermal cells which lies close to the growing root tip. It is likely that this transient, nodulation (nod) gene-dependent activation of the ENOD12 gene also corresponds to the preparation of the plant for bacterial infection. We anticipate that this extremely precocious response to Rhizobium will provide a valuable molecular marker for studying early signal exchange between the two symbiotic organisms.

138 NAL Call. No.: 450 P692 RNA editing of cytochrome oxidase subunit III in sunflower mitochondria. Saiardi, A.; Quagliariello, C.
Rockville, Md. : American Society of Plant Physiologists; 1992 Apr. Plant physiology v. 98 (4): p. 1261-1263; 1992 Apr. Includes references.

Language: English

Descriptors: Helianthus annuus; Mitochondria; Messenger RNA; Transcription; Cytochrome-c oxidase; Nucleotide sequences; Gene expression; Genome analysis

Abstract: Direct sequencing of cytochrome oxidase subunit III (coxIII) mRNA with a specific primer confirms RNA editing in sunflower (Helianthus annus) mitochondria. Six instances of mRNA editing could be verified, one of these specific to this species. All the editing events involve C to U transitions in the coxIII mRNA causing codon changes that lead to amino acids better conserved in evolution than those encoded in the genomic DNA. This observation confirms RNA editing to be widespread in higher plant mitochondria.

139 NAL Call. No.: QH506.E46 Roles of plant homologs of Rab1p and Rab7p in the biogenesis of the peribacteroid membrane, a subcellular compartment formed de novo during root nodule symbiosis.
Cheon, C.I.; Lee, N.G.; Siddique, A.B.M.; Bal, A.K.; Verma, D.P.S. Oxford, Eng. : Oxford University Press; 1993 Nov. The EMBO journal v. 12 (11): p. 4125-4135; 1993 Nov. Includes references.

Language: English

Descriptors: Glycine max; Vigna aconitifolia; Bradyrhizobium japonicum; Plant proteins; Binding proteins; Guanosine triphosphate; Cell membranes; Cell differentiation; Root nodules; Complementary DNA; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Nodulation; Genetic regulation; Antisense RNA; Transgenic plants; Genetic transformation

Abstract: The peribacteroid membrane (PBM) in legume root nodules is derived from plasma membrane following endocytosis of Rhizobium by fusion of newly synthesized vesicles. We studied the roles of plant Rab1p and Rab7p homologs, the small GTP-binding proteins involved in vesicular transport, in the biogenesis of the PBM. Three cDNAs encoding legume homologs of mammalian Rab1p and Rab7p were isolated from soybean (sRab1p, sRab7p) and Vigna aconitifolia (vRab7p). sRab1p was confirmed to be a functional counterpart of yeast Ypt1p (Rab1p) by complementation of a yeast ypt1-1 mutant. Both srab1 and vrab7 genes are induced during nodulation with the level of vrab7 mRNA being 12 times higher than that in root meristem and leaves. This induction directly correlates with membrane proliferation in nodules. Antisense constructs of srab1 and vrab7, under a nodule-specific promoter (leghemoglobin, Lbc3), were made in a binary vector and transgenic nodules were developed on soybean hairy roots obtained through Agrobacterium rhizogenes-mediated transformation. Both antisense srab1 and vrab7 nodules were smaller in size and showed lower nitrogenase activity than controls. The antisense srab1 nodules showed lack of expansion of infected cells, fewer bacteroids per cell and their frequent release into vacuoles. In contrast, antisense vrab7 expressing nodules showed accumulation of late endosomal structures and multivesicular bodies in the perinuclear region. These data suggest that both Rab1p and Rab7p are essential for the development of the PBM compartment in effective symbiosis.

140 NAL Call. No.: 450 P564 Root nodule development: origin, function and regulation of nodulin genes. Verma, D.P.S.; Hu, C.A.; Zhang, M.
Copenhagen : The Scandinavian Society for Plant Physiology; 1992 Jun. Physiologia plantarum v. 85 (2): p. 253-265; 1992 Jun. Includes references.

Language: English

Descriptors: Leguminosae; Rhizobium; Gene expression; Nodulins; Structural genes; Nodulation; Root nodules; Cell differentiation; Bacteroids

Abstract: The symbiotic root nodule, an organ formed on leguminous plants, is a product of successful interactions between the host plant and the soil bacteria, Rhizobium spp. Plant hormones play an important role in the genesis of this organ. The hormonal balance appears to be modulated by the signals produced by bacteria. Many host genes induced during nodule organogenesis and the symbiotic state have been identified and characterized from several legumes. These genes encode nodule-specific proteins (nodulins) which perform diverse functions in root nodule development and metabolism. Formation of a subcellular compartment housing the bacteria is essential to sustain the symbiotic state, and several nodulins arc involved in maintaining the integrity and function of this compartment. The bacteroid enclosed in the peribacteroid membrane behaves as an 'organelle,' completely dependent on the host for all its requirements for carbon, nitrogen and other essential elements. Thus it seems likely that the nodulins in the peribacteroid membrane perform specific transport functions. While the function of a few other nodulins is known (e.g. nodulin-100, nodulin-35), a group of uncharacterized nodulins exists in soybean root nodules. These nodulins share structural similarities and seem to have been derived from a common ancestor. Induction of nodulin genes occurs prior to and independent of nitrogen fixation, and thus is a prelude to symbiosis. Although some of the early nodulin genes are induced prior to or during infection, induction of late nodulins requires endocytotic release of bacteria.

141 NAL Call. No.: QK710.P62 Seed-specific repression of GUS activity in tobacco plants by antisense RNA. Fujiwara, T.; Lessard, P.A.; Beachy, R.N. Dordrecht : Kluwer Academic Publishers; 1992 Dec. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 20 (6): p. 1059-1069; 1992 Dec. Includes references.

Language: English

Descriptors: Nicotiana tabacum; Transgenics; Genetic transformation; Beta-glucuronidase; Reporter genes; Recombinant DNA; Promoters; Plant proteins; Gene expression; Genetic regulation; Antisense RNA; Seeds; Messenger RNA; Enzyme activity

Abstract: beta-Conglycinin, the 7S storage protein of soybean, is expressed only in seeds and is regulated predominantly by gene transcription. We applied an antisense strategy to modify expression of a beta-glucuronidase (uidA or gusA) gene in seeds using a promoter from a beta-conglycinin gene. Transgenic tobacco plants harboring the gusA gene under the control of the CaMV 35S promoter were retransformed with a gene construct comprising the beta-conglycinin promoter fused to the gusA gene in the antisense orientation. Double transformants were regenerated and transformation was confirmed by Southern blot hybridization. Seed-specific repression of GUS activity was observed in lines containing high copy numbers of the antisense gusA transgene. Suppression of GUS activity was correlated with the amounts of (-) sense gusA transcript detected and concomitantly with a decrease in gusA transcript levels. Furthermore, the amount of suppression of GUS activity was greatest during mid to late stages of seed development, when expression of the alpha' promoter is high. These results indicate that suppression of GUS activity is due to expression of the antisense gene.

142 NAL Call. No.: QK710.P62 Sequence analysis and developmental expression of an alfalfa protein disulfide isomerase.
Shorrosh, B.S.; Dixon, R.A.
Dordrecht : Kluwer Academic Publishers; 1992 May. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (2): p. 319-321; 1992 May. Includes references.

Language: English

Descriptors: Medicago sativa; Structural genes; Dna; Isomerases; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Plant development

143 NAL Call. No.: QK710.P62 Sequence and transcription analysis of mitochondrial plasmids isolated from cytoplasmic male-sterile lines of Vicia faba. Flamand, M.C.; Goblet, J.P.; Duc, G.; Briquet, M.; Boutry, M. Dordrecht : Kluwer Academic Publishers; 1992 Sep. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (6): p. 913-923; 1992 Sep. Includes references.

Language: English

Descriptors: Vicia faba; Mitochondrial DNA; Plasmids; Cytoplasmic male sterility; Nucleotide sequences; Transcription; Gene expression; Messenger RNA; Southern blotting; Dna; Nuclei

Abstract: Three mitochondrial plasmids (1704, 1695 and 1478 bp) were isolated from sterile cytoplasms of Vicia faba L. and cloned into a bacterial plasmid vector. Their nucleotide sequence was found to be 99 to 100% homologous to their counterparts isolated from a fertile cytoplasm (J.A. Wahleithner and D.R. Wolstenholme, Curr Genet 12 (1987) 55-76). Several overlapping transcripts were localized in the region which is unique to each of the three plasmids. S1 nuclease mapping indicated for all of them several 3' termini but a unique 5' boundary which was located downstream of the consensus sequence CNTAAGTGANNNNNGAA also found at the transcript 5' boundary of other plant mitochondrial plasmids. Southern blot hybridization with nuclear DNA indicated the presence of nuclear sequences homologous to each plasmid.

144 NAL Call. No.: 450 P692 Sequence of a Brassica campestris myrosinase gene. Machlin, S.; Mitchell-Olds, T.; Bradley, D. Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug. Plant physiology v. 102 (4): p. 1359-1360; 1993 Aug. Includes references.

Language: English

Descriptors: Brassica campestris; Structural genes; Thioglucosidase; Nucleotide sequences; Amino acid sequences; Introns; Multigene families; Gene expression; Messenger RNA

145 NAL Call. No.: QK710.P62 Sequence of cab-151, a gene encoding a photosytem II type II chlorophyll a/b-binding protein in cotton.
Sagliocco, F.; Kapazoglou, A.; Dure L. III Dordrecht : Kluwer Academic Publishers; 1992 Feb. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 18 (4): p. 841-842; 1992 Feb. Includes references.

Language: English

Descriptors: Gossypium hirsutum; Genes; Chlorophyll a/b binding protein; Nucleotide sequences; Amino acid sequences; Photosystem ii; Introns; Gene expression; Messenger RNA; Leaves; Cotyledons

146 NAL Call. No.: SB732.6.M65 Sequential expression of two late nodulin genes in the infected cells of alfalfa root nodules.
Allen, T.; Raja, S.; Ganter, G.; Dunn, K. St. Paul, Minn. : APS Press; 1992 Sep.
Molecular plant-microbe interactions : MPMI v. 5 (5): p. 430-434; 1992 Sep. Includes references.

Language: English

Descriptors: Medicago sativa; Root nodules; Nodulation; Symbiosis; Genes; Nodulins; Gene expression; Leghemoglobin; Nitrogen fixation

147 NAL Call. No.: QK725.I43 A short histone H3 promoter from alfalfa specifies expression in S-phase cells and meristems.
Kapros, T.; Stefanov, I.; Magyar, Z.; Ocsovszky, I.; Dudits, D. Columbia, MD : Tissue Culture Association; 1993 Jan. In vitro cellular & developmental biology : plant v. 29P (1): p. 27-32; 1993 Jan. Includes references.

Language: English

Descriptors: Medicago sativa; Nicotiana tabacum; Medicago varia; Promoters; Histones; Recombinant DNA; Beta-glucuronidase; Reporter genes; Transgenic plants; Genetic transformation; Gene expression; Cell division; Shoot meristems; Histoenzymology

148 NAL Call. No.: QK756.A28 1992 Signal transduction and gene expression during cold acclimation of alfalfa. Dhindsa, R.S.; Monroy, A.; Wolfraim, L.; Dong, G. Boca Raton : CRC Press; 1992.
Advances in plant cold hardiness / edited by Paul H. Li, Lars Christersson. p. 57-71; 1992. Key papers presented at the "4th International Plant Cold Hardiness Seminar" and the invitational papers at the Swedish University of Agricultural Sciences, July 1 to 5, 1991, Uppsala. Includes references.

Language: English

Descriptors: Medicago sativa; Cold tolerance; Gene expression; Transduction

149 NAL Call. No.: QH506.E46 Silent mitochondrial and active nuclear genes for subunit 2 of cytochrome c oxidase (cox2) in soybean: evidence for RNA-mediated gene transfer. Covello, P.S.; Gray, M.W.
Oxford, Eng. : IRL Press; 1992 Nov.
The EMBO journal - European Molecular Biology Organization v. 11 (11): p. 3815-3820; 1992 Nov. Includes references.

Language: English

Descriptors: Glycine max; Mitochondrial DNA; Structural genes; Cytochrome-c oxidase; Nuclei; Mitochondrial genetics; Gene expression; Transcription; Nucleotide sequences; Introns; Amino acid sequences; Rna editing; Evolution

Abstract: In most plants and other eukaryotes investigated, the mitochondrial genome carries the gene encoding subunit 2 of cytochrome c oxidase (cox2). In this paper, we show that the previously reported mitochondrial cox2 of soybean is actually silent, and that there is an expressed, single-copy, nucleus-encoded cox2. Molecular cloning and sequence analysis of cox2 cDNA and genomic clones show that the soybean nuclear gene encodes an N-terminal extension that resembles a signal sequence for mitochondrial import and whose coding sequence is separated by an intron from that corresponding to mtDNA-encoded cox2. Comparison of soybean mitochondrial and nuclear cox2 sequences clearly indicates that in an ancestor of soybean, cox2 was transferred from the mitochondrion to the nucleus via a C-to-U edited RNA intermediate.

150 NAL Call. No.: QK710.P68 Site-directed mutagenesis of the organ-specific element in the soybean leghemoglobin lbc3 gene promoter.
Ramiov, K.B.; Laursen, N.B.; Stougaard, J.; Marcker, K.A. 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. 577-580; 1993 Sep. Includes references.

Language: English

Descriptors: Glycine max; Lotus corniculatus; Gene expression; Genetic transformation; Leghemoglobin; Mutagenesis; Nucleotide sequences; Promoters

151 NAL Call. No.: QK710.P62 A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules. Madsen, O.; Sandal, L.; Sandal, N.N.; Marcker, K.A. Dordrecht : Kluwer Academic Publishers; 1993 Oct. Plant molecular biology v. 23 (1): p. 35-43; 1993 Oct. Includes references.

Language: English

Descriptors: Glycine max; Complementary DNA; Structural genes; Oxidoreductases; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Root nodules; Leaves

Abstract: In plants the enzyme coproporphyrinogen oxidase catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX in the heme and chlorophyll biosynthesis pathway(s). We have isolated a soybean coproporphyrinogen oxidase cDNA from a cDNA library and determined the primary structure of the corresponding gene. The coproporphyrinogen oxidase gene encodes a polypeptide with a predicted molecular mass of 43 kDa. The derived amino acid sequence shows 50% similarity to the corresponding yeast amino acid sequence. The main difference is an extension of 67 amino acids at the N-terminus of the soybean polypeptide which may function as a transit peptide. A full-length coproporphyrinogen oxidase cDNA clone complements a yeast mutant deleted of the coproporphyrinogen oxidase gene, thus demonstrating the function of the soybean protein. The soybean coproporphyrinogen oxidase gene is highly expressed in nodules at the stage where several late nodulins including leghemoglobin appear. The coproporphyrinogen oxidase mRNA is also detectable in leaves but at a lower level than in nodules while no mRNA is detectable in roots. The high level of coproporphyrinogen oxidase mRNA in soybean nodules implies that the plant increases heme production in the nodules to meet the demand for additional heme required for hemoprotein formation.

152 NAL Call. No.: 450 P699 Soybean lipoxygenase L-4, a component of the 94-kilodalton storage protein in vegetative tissues: expression and accumulation in leaves induced by pod removal and by methyl jasmonate.
Kato, T.; Shirano, Y.; Iwamoto, H.; Shibata, D. Kyoto, Japan : Japanese Society of Plant Physiologists; 1993 Oct. Plant and cell physiology v. 34 (7): p. 1063-1072; 1993 Oct. Includes references.

Language: English

Descriptors: Glycine max; Leaves; Plant tissues; Pods; Amino acid sequences; Lipoxygenase; Nucleotide sequences; Plant proteins; Cloning; Gene expression; Genetic code; Jasmonic acid

Abstract: A lipoxygenase L-4 gene was isolated from a soybean genomic library. The amino acid sequence of lipoxygenase L-4 is highly homologous with the partial amino acid sequence of the 94-kDa vegetative storage protein, vsp94, found in paraveinal mesophyll cells in the leaves of depodded soybean plants. No L4 expression was observed in maturing seeds. The L4 gene is highly expressed in the vegetative tissues of young seedlings, including cotyledons, hypocotyls, roots and primary leaves. L-4 expression followed the same pattern as lipoxygenase activity in cotyledons peaking 3 to 5 days after germination, and returning to a basal level by 9 days after germination. L-4 gene expression was low in the roots, stems and leaves of 10-week-old plants. Exposure of 4-week-old plants to atmospheric methyl jasmonate increased L-4 mRNA in leaves. Continuous pod removal from 7-week-old plants over a 2 week period resulted in dramatic accumulation of L-4 mRNA in leaves. Accumulation of the L-4 protein and three other lipoxygenase fractions in the leaves of depodded plants was demonstrated by ion exchange chromatography. These results indicate that lipoxygenase L-4 is a component of vsp94.

153 NAL Call. No.: QK725.P532 Soybean nodulin-26 gene encoding a channel protein is expressed only in the infected cells of nodules and is regulated differently in roots of homologous and heterologous plants.
Miao, G.H.; Verma, D.P.S.
Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Jul. The Plant cell v. 5 (7): p. 781-794; 1993 Jul. Includes references.

Language: English

Descriptors: Glycine max; Multigene families; Structural genes; Nodulins; Nucleotide sequences; Amino acid sequences; Gene expression; Messenger RNA; Root nodules; Roots; Introns; Exons; Promoters; Transgenic plants; Genetic transformation; Nicotiana tabacum; Lotus corniculatus; Root meristems; Complementary DNA

Abstract: Nodulin-26 (N-26) is a major peribacteroid membrane protein in soybean root nodules. The gene encoding this protein is a member of an ancient gene family conserved from bacteria to humans. N-26 is specifically expressed in root nodules, while its homolog, soybean putative channel protein, is expressed in vegetative parts of the plant, with its highest level in the root elongation zone. Analysis of the soybean N-26 gene showed that its four introns mark the boundaries between transmembrane domains and the surface peptides, suggesting that individual transmembrane domains encoded by a single exon act as functional units. The number and arrangement of introns between N-26 and its homologs differ, however. Promoter analysis of N-26 was conducted in both homologous and heterologous transgenic plants. The cis-acting elements of the N-26 gene are different from those of the other nodulin genes, and no nodule-specific cis-acting element was found in this gene. in transgenic nodules, the expression of N-26 was detected only in the infected cells; no activity was found in nodule parenchyma and uninfected cells of the symbiotic zone. The N-26 gene is expressed in root meristem of transgenic Lotus corniculatus and tobacco but not in untransformed and transgenic soybean roots, suggesting the possibility that this nodulin gene is controlled by a trans-negative regulatory mechanism in homologous plants. This study demonstrates how a preexisting gene in the root may have been recruited for symbiotic function and brought under nodule-specific developmental control.

154 NAL Call. No.: 450 P692 Soybean seed coat peroxidase: a comparison of high-activity and low-activity genotypes.
Gijzen, M.; Van Huystee, R.; Buzzell, R.I. Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Dec. Plant physiology v. 103 (4): p. 1061-1066; 1993 Dec. Includes references.

Language: English

Descriptors: Glycine max; Testas; Plant composition; Peroxidase; Enzyme activity; Genetic regulation; Genotypes; Genetic variation; Cultivars; Roots; Gene expression; Alleles; Histochemistry; Plant anatomy

Abstract: Peroxidase activity in the seed coats of soybean (Glycine max [L.] Merr.) is controlled by the Ep locus. We compared peroxidase activity in cell-free extracts from seed coat, root, and leaf tissues of three EpEp cultivars (Harosoy 63, Harovinton, and Coles) to three epep cultivars (Steele, Marathon, and Raiden). Extracts from the seed coats of EpEp cultivars were 100-fold higher in specific activity than those from epep cultivars, but there was no difference in specific activity in crude root or leaf extracts. Isoelectric focusing of root tissue extracts and staining for peroxidase activity showed that EpEp cultivars had a root peroxidase of identical isoelectric point to the seed coat peroxidase, whereas roots of the epep types were lacking that peroxidase, indicating that the Ep locus may also affect expression in the root. In seed coat extracts, peroxidase was the most abundant soluble protein in EpEp cultivars, whereas this enzyme was present only in trace amounts in epep genotypes, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Histochemical localization of peroxidase activity inseed coats of EpEp cultivars shows that the enzyme occurs predominately in the cytoplasm of hourglass cells of the subepidermis. No obvious difference in the gross or microscopic structure of the seed coat was observed to be associated with the Ep locus. These results suggest that soybean seed coat peroxidase may be involved in processes other than seed coat biosynthesis.

155 NAL Call. No.: 381 J824 A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation. Kalinski, A.; Melroy, D.L.; Dwivedi, R.S.; Herman, E.M. Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1992 Jun15.
The Journal of biological chemistry v. 267 (17): p. 12068-12076; 1992 Jun15. Includes references.

Language: English

Descriptors: Glycine max; Seeds; Seed maturation; Thiols; Proteinases; Gene expression; Protein synthesis; Glycoproteins; Precursors; Organelles

Abstract: We have examined the synthesis, posttranslational processing, and localization of soybean P34, a member of the papain superfamily. P34 has been identified as a constituent of oil storage organelles or oil bodies isolated from seed lysates and has been assumed to be one of the oil body proteins. Electron microscopic immunocytochemistry with a monoclonal antibody demonstrated that P34 is localized in the protein storage vacuoles but not in the oil bodies. Immunocytochemical observations of partially disrupted seed cells showed that the association of P34 with oil bodies appears to occur as a consequence of cell lysis. In vitro synthesis of P34 results in the formation of a 46-kDa polypeptide that increases to 47 kDa due to core glycosylation by canine microsomes. In vivo synthesis studies in the presence and absence of tunicamycin, an inhibitor of N-linked glycosylation, indicate that pro-P34 is 47 kda. Since the cDNA sequence of prepro-P34 contains a single putative glycosylation site in the precursor domain, we conclude that P34, like a few other vacuolar proteins, is synthesized as a glycoprotein precursor. Pulse-chase experiments showed that the processing of pro-P34 to mature P34 occurs in a single step and that this posttranslational cleavage occurs on the carboxyl side of an Asn, which is typical of seed vacuolar proteins. Pro-P34 (47 kDa) is detected in immunoblots of maturing seeds. Analysis of RNA indicates that the P34 genes are expressed only during seed maturation and that the P34 mRNA is related to other thiol protease mRNAs detectable in other organs and plants. Unlike other seed thiol proteases that are synthesized only after seed germination, P34 accumulates during seed maturation.

156 NAL Call. No.: 450 P693 Spatial and temporal expression of Cab mRNAs in cotyledons of the developing soybean seedling.
Chang, Y.C.; Walling, L.L.
Secaucus, N.J. : Springer-Verlag; 1992. Planta v. 186 (2): p. 262-272; 1992. Includes references.

Language: English

Descriptors: Glycine max; Seedlings; Developmental stages; Cotyledons; Messenger RNA; Gene expression; Genetic code; Chlorophyll a/b binding protein; Spatial distribution; Plant anatomy

Abstract: Changes in the temporal and spatial distribution of the mRNAs for the chlorophyll-a/b-binding-protein gene (Cab) in cotyledons from developing soybean (Glycine max (L.) Merr.) seedlings were studied. Cab mRNAs could be detected in the polysomal polyadenylated poly(A)+ mRNA population of cotyledons within 3 d after start of imbibition, prior to their emergence from soil, and declined prior to the onset of cotyledonary senescence. The Cab mRNA levels were compared to the levels of rbcS (ribulose-1,5-bisphosphate carboxylase small subunit) mRNAs in cotyledons and distinct differences in their expression programs were noted. Quantitative analyses with S1 nuclease were used to monitor the accumulation of the mRNAs of individual members of the Cab gene family. Cab 3, Cab 4, and Cab 5 mRNAs were differentially regulated in the cotyledons during post-germinative development. Cab 4 was the most abundant Cab gene mRNA representing approx. 4.3% of the cotyledonary polysomal poly(A)+ mRNA population. In-situ hybridizations using methacrylate-imbedded tissue and 3H-antisense- and -sense-strand RNA probes were used to determine the qualitative and quantitative distribution of Cab RNAs in cotyledonary cells. Cab RNAs were most abundant in the palisade cells. These results indicate an interaction of both developmental and environmental cues in modulating the expression of the Cab gene family in soybean cotyledons.

157 NAL Call. No.: QK710.P62 Stress response in alfalfa (Medicago sativa L.). 15. Characterization and expression patterns of members of a subset of the chalcone synthase multigene family.
Junghans, H.; Dalkin, K.; Dixon, R.A.
Dordrecht : Kluwer Academic Publishers; 1993 May. Plant molecular biology v. 22 (2): p. 239-253; 1993 May. Includes references.

Language: English

Descriptors: Medicago; Multigene families; Structural genes; Naringenin-chalcone synthase; Complementary DNA; Nucleotide sequences; Amino acid sequences; Messenger RNA; Gene expression; Roots; Root nodules; Stems; Leaves; Flowers; Genetic regulation; Abiotic injuries; Cell wall components; Fungal diseases; Phoma medicaginis; Cell suspensions

Abstract: We have identified five different full length chalcone synthase (CHS) cDNA clones from a cDNA library produced from transcripts isolated from an elicitor-treated alfalfa cell suspension culture. Nucleotide sequence similarity between the clones varied from 88-93%. Oligonucleotides based on divergent se- quences in the 5'-untranslated regions of the clones could distinguish individual genes, or groups of genes and their corresponding transcripts. Developmentally regulated expression of the CHS transcripts was predominantly in roots and root nodules; other unidentified members of the CHS gene family are expressed in stems, leaves and nodules. One of the CHS transcripts was strongly expressed in floral tissue. All the CHS transcripts studied were induced in elicitor-treated cell suspension cultures. Transcripts were also induced in roots in response to wounding or spraying with various elicitors, and in leaves infected with Phoma medicaginis (but not in wounded leaves). The induction kinetics of CHS2 transcripts were more rapid and/or transient than those of other members of the CHS family in CuCl2-treated roots and Phoina-infected leaves. The results are discussed in terms of the evolution and functions of the CHS gene family in legumes.

158 NAL Call. No.: 381 Ar2 Stress responses in alfalfa (Medicago sativa L.) XVII: molecular cloning and expression of the elicitor-inducible cinnamic acid 4-hydroxylase cytochrome P450.
Fahrendorf, T.; Dixon, R.A.
Orlando, Fla. : Academic Press; 1993 Sep. Archives of biochemistry and biophysics v. 305 (2): p. 509-515; 1993 Sep. Includes references.

Language: English

Descriptors: Medicago sativa; Cell suspensions; Cytochrome p-450; Stress; Phytoalexins; Gene expression; Cloning; Nucleotide sequences; Amino acid sequences

Abstract: We have isolated cDNA clones encoding a novel class of plant cytochrome P450 by screening an alfalfa cDNA expression library with an antibody against an avocado P450 (CYP73A1) that is expressed during fruit ripening but that has not yet been ascribed an in vivo activity. The cDNAs encode a polypeptide of Mr 58,000, pI 9.3, containing sequence similarity (25 to 31% overall at the amino acid level) to the avocado P450 and mammalian, yeast, and bacterial P450s, particularly in the presumed heme binding region. Expression studies in yeast confirmed that the P450 clones encode cinnamic acid 4-hydroxylase (CA4H), a key enzyme of the phenylpropanoid pathway in plants. CA4H is encoded by a small gene family in alfalfa, which does not appear to contain homologs of the avocado P450. CA4H transcripts are strongly induced by fungal elicitor at the onset of accumulation of isoflavonoid phytoalexins in alfalfa cell suspension cultures.

159 NAL Call. No.: 450 P692 Subcellular location of delta-1-pyrroline-5-carboxylase reductase in root/nodule and leaf of soybean.
Szoke, A.; Miao, G.H.; Hong, Z.; Verma, D.P.S. Rockville, Md. : American Society of Plant Physiologists; 1992 Aug. Plant physiology v. 99 (4): p. 1642-1649; 1992 Aug. Includes references.

Language: English

Descriptors: Glycine max; Roots; Root nodules; Leaves; Chemical composition; Oxidoreductases; Enzyme activity; Proline; Biosynthesis; Genetic regulation; Gene expression; Escherichia coli; Gene transfer; Nicotiana tabacum; Transgenics; Genetic transformation; Carboxylic acids

Abstract: The expression of delta-1-pyrroline-5-carboxylate reductase (P5CR) gene was found to be higher in soybean root nodules than in leaves and roots, and its expression in roots appeared to be osmoregulated (AJ Delauney, DPS Verma [1990] Mol Gen Genet 221: 299-305). P5CR was purified to homogeneity as a monomeric protein of 29 kilodaltons by overexpression of a soybean P5CR cDNA clone in Escherichia coli. The pH optimum of the purified P5CR was altered by increasing the salt concentration, and maximum enzyme activity was attainable at a lower pH under high salt (0.2-1 molar NaCl). Kinetic studies of the purified enzyme suggested that nicotinamide adenine dinucleotide phosphate+ inhibited P5CR activity, whereas nicotinamide adenine dinucleotide+ did not. Subcellular fractionation and antibodies raised against purified soybean P5CR were used to investigate location of the enzyme in different parts of soybean as well as in leaves of transgenic tobacco plants synthesizing soybean P5CR. P5CR activity was present in cytoplasm of soybean roots and nodules as well as in leaves, but in leaves, about 15% of the activity was detected in the plastid fraction. The location of P5CR was further confirmed by western blot assay of the proteins from cytosol and plastid fractions of different parts of the plant. Expression of soybean nodule cytosolic P5CR in transgenic tobacco under the control of cauliflower mosaic virus 35S promoter led to the accumulation of this protein exclusively in the cytoplasm, suggesting that the chloroplastic activity may be due to the presence of a plastid form of the enzyme. The different locations of P5CR in root and leaf suggested that proline may be synthesized in different subcellular compartments in root and leaf. Proline concentration was not significantly increased in transgenic plants exhibiting high level P5CR activity, indicating that reduction of P5C is not a rate-limiting step in proline production.

160 NAL Call. No.: SB732.6.M65 The sucrose synthase gene is predominantly expressed in the root nodule tissue of Vicia faba.
Kuster, H.; Fruhling, M.; Perlick, A.M.; Puhler, A. St. Paul, Minn. : APS Press; 1993 Jul.
Molecular plant-microbe interactions : MPMI v. 6 (4): p. 507-514; 1993 Jul. Includes references.

Language: English

Descriptors: Vicia faba; Structural genes; Complementary DNA; Sucrose synthase; Nucleotide sequences; Amino acid sequences; Gene expression; Root nodules; Messenger RNA

161 NAL Call. No.: 450 P693 A sucrose-synthase gene of Vicia faba L.: Expression pattern in developing seeds in relation to starch synthesis and metabolic regulation. Heim, U.; Weber, H.; Baumlein, H.; Wobus, U. Berlin ; New York : Springer-Verlag, 1925-; 1993. Planta v. 191 (3): p. 394-401; 1993. Includes references.

Language: English

Descriptors: Vicia faba; Seed development; Starch; Biosynthesis; Metabolism; Sucrose synthase; Genetic regulation; Genetic code; Gene expression; Protein synthesis; Nucleotide sequences; Amino acid sequences; Plant composition

Abstract: Copy-DNA clones encoding a single class of sucrose-synthase (SUCS; EC 2.4.1.13) subunit have been isolated and sequenced from a Vicia faba L. seed cotyledonary library. Southern analyses indicated the existence of only one gene. Transcript levels determined by Northern blot hybridisation steadily increased until the middle of development [25-35 days after flowering (DAF)] and declined thereafter. Sucrose levels approximately paralleled levels of SUCS mRNA. The activity of SUCS increased with decreasing fructose and glucose concentrations and peaked about 10 d later than mRNA levels. In-vitro culture experiments demonstrated that increasing the sucrose concentration leads to increased levels of SUCS mRNA. The SUCS mRNA was also synthesised in seed-coat tissue, but in lower amounts than in cotyledons and with a different developmental profile. The early peak level of SUCS mRNA (20 DAF) in seed coats coincided with the peak in the amount of sucrose and with a peak of transiently synthesised starch.

162 NAL Call. No.: QK710.P62 Suppression of gene expression in plant cells utilizing antisense sequences transcribed by RNA polymerase III.
Bourque, J.E.; Folk, W.R.
Dordrecht : Kluwer Academic Publishers; 1992 Jul. Plant molecular biology : an international journal on molecular biology, biochemistry and genetic engineering v. 19 (4): p. 641-647; 1992 Jul. Includes references.

Language: English

Descriptors: Glycine max; Daucus carota; Antisense DNA; Recombinant DNA; Transfer RNA; Methionine; Reporter genes; Chloramphenicol acetyltransferase; Regulation; Gene expression; Rna polymerase; Enzyme activity; Transcription; Rna

Abstract: Inverted sequences of the chloramphenicol acetyltransferase (CAT) reporter gene were fused to a soybean tRNA(met(i)) gene lacking a terminator such that the tRNA(met(i)) sequences caused the co-transcription of CAT antisense sequences by RNA polymerase III. When electroporated into carrot protoplasts, these antisense DNA constructs suppressed CAT enzyme activity expressed from co-electroporated DNAs containing the CAT gene downstream of the cauliflower mosaic virus (CaMV) 35S RNA promoter. Our most effective construct, an antisense sequence complementary to the 3' portion of the CAT gene, inhibited CAT activity five-fold greater than an antisense construct expressed by RNA polymerase II from the cauliflower mosaic virus 35S RNA promoter. These results indicate that antisense sequences transcribed by RNA polymerase III should efficiently suppress gene expression in plants.

163 NAL Call. No.: QK710.P62 A survey of transcripts expressed specifically in root nodules of broadbean (Vicia faba L.).
Perlick, A.M.; Puhler, A.
Dordrecht : Kluwer Academic Publishers; 1993 Sep. Plant molecular biology v. 22 (6): p. 957-970; 1993 Sep. Includes references.

Language: English

Descriptors: Vicia faba; Messenger RNA; Transcription; Root nodules; Gene expression; Complementary DNA; Dna libraries; Nodulins; Leghemoglobin; Plant proteins; Sucrose synthase; Aspartate-ammonia ligase; Lipoxygenase

Abstract: More than 600 potentially nodule-specific clones have been detected by differential hybridization of a broadbean cDNA library constructed from root nodule poly(A)(+) RNA. These isolated cDNAs belong to at least 28 different clone groups containing cross-hybridizing sequences. The number of clones within a clone group varies from about 200 to only one single clone. Northern hybridization experiments revealed nodule-specific transcripts for 14 clone groups and markedly nodule-enhanced transcripts for another 7 clone groups. Sequence homologies indicate that three transcript sequences code for different leghemoglobins. Two other transcripts encode a nodule-specific sucrose synthase and a nodule-enhanced asparagine synthetase, respectively. Four deduced gene products are proline-rich, two of them being the homologues of PsENOD2 and PsENOD12. The third proline-rich protein (PRP) is composed of similar amino acid repeats as the nodule-specific PsENOD12 but is expressed in nodules and roots in comparable amounts. The fourth PRP is a nodule-enhanced extensin-type protein built up by Ser-Pro4 repeats. Two further nodule-specific transcripts encode gene products showing some similarity to structural glycine-rich proteins. Additionally, transcripts could be identified for broadbean homologues of the nodulins MsNOD25, PsENOD3 and PsENOD5 and transcripts specifying a nodule-enhanced lipoxygenase and a translation elongation factor EF-1alpha, which is expressed in all broadbean tissues tested.

164 NAL Call. No.: QD415.F4 Thermal injury and ozone stress affect soybean lipoxygenases expression. Maccarrone, M.; Veldink, G.A.; Vliegenthart, J.F.G. Amsterdam, Netherlands : Elsevier Science Publishers; 1992 Sep14. F E B S letters : Federation of European Biochemical Societies v. 309 (3): p. 225-230; 1992 Sep14. Includes references.

Language: English

Descriptors: Glycine max; Structural genes; Lipoxygenase; Isoenzymes; Gene expression; Transcription; Messenger RNA; Genetic regulation; Ozone; Heat shock; Cold shock; Enzyme activity; Seedlings; Cold stress; Heat stress; Translation

Abstract: The effects of thermal injury (cold and heat shock) and ozone treatment on lipoxygenases 1 (LOX-1) and 2 (LOX-2) of soybean seedlings have been investigated. Cold stress led to a decrease of the specific activities of both isoenzymes, attributable at least in part to a down-regulation of gene expression at the translational level. Both heat shock and ozone treatment enhanced lipoxygenases-specific activities, acting at the level of transcription of the genes. It is proposed that LOX-1 and LOX-2 are involved in the thermotolerance of soybeans and in the precocious aging induced by ozone.

165 NAL Call. No.: QK710.P68 Tissue-specific expression of sunflower heat shock proteins in response to water stress.
Almoguera, C.; Coca, M.A.; Jordano, J.
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. 947-958; 1993 Dec. Includes references.

Language: English

Descriptors: Helianthus annuus; Gene expression; Genetic code; Heat shock proteins; Messenger RNA; Protein synthesis; Responses; Water stress

166 NAL Call. No.: 450 P692 Tissue-specific expression of the alternative oxidase in soybean and siratro. Kearns, A.; Whelan, J.; Young, S.; Elthon, T.E.; Day, D.A. Rockville, Md. : American Society of Plant Physiologists; 1992 Jun. Plant physiology v. 99 (2): p. 712-717; 1992 Jun. Includes references.

Language: English

Descriptors: Glycine max; Macroptilium atropurpureum; Bradyrhizobium japonicum; Bradyrhizobium; Shoots; Roots; Root nodules; Oxidoreductases; Enzyme activity; Respiration; Mitochondria; Gene expression; Genetic regulation; Protein synthesis

Abstract: Alternative oxidase activity (cyanide-insensitive respiration) was measured in mitochondria from the shoots, roots, and nodules of soybean (Glycine max L.) and siratro (Macroptilium atropurpureum) plants. Activity was highest in the shoots and lowest in the nodules. Alternative oxidase activity was associated with one (roots) or two (shoots) proteins between 30 and 35 kilodaltons that were detected by western blotting with a monoclonal antibody against Sauromatum guttatum alternative oxidase. No such protein was detected in nodule mitochondria. Measurements of oxygen uptake by isolated soybean root and nodule cells in the presence of cyanide and salicylhydroxamic acid indicated that alternative oxidase activity was confined to the uninfected cortex cells of the nodule. Immunoprecipitation of translation products of mRNA isolated from soybean shoots revealed a major band at 43 kilodaltons that is assumed to be the precursor of an alternative oxidase protein. This band was not seen when mRNA from nodules was treated in the same fashion. The results indicate that tissue-specific expression of the alternative oxidase occurs in soybean and siratro.

167 NAL Call. No.: S494.5.B563C87 Transcriptional regulation of auxin-responsive genes. Gulfoyle, T.J.; Hagen, G.; Li, Y.; Gee, M.A.; Martin, G.; Ulmasov, T.N. Dordrecht : Kluwer Academic Publishers; 1992. Current plant science and biotechnology in agriculture v. 13: p. 129-135; 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: Glycine max; Structural genes; Multigene families; Promoters; Plant proteins; Gene expression; Messenger RNA; Genetic regulation; Auxins

168 NAL Call. No.: S494.5.B563C87 Transcriptional regulation of phytoalexin biosynthetic genes. Dixon, R.A.; Bhattacharyya, M.K.; Harrison, M.J.; Faktor, O.; Lamb, C.J.; Loake, G.J.; Ni, W.; Oommen, A.; Paiva, N.; Stermer, B. Dordrecht : Kluwer Academic Publishers; 1993. Current plant science and biotechnology in agriculture v. 14: p. 497-509; 1993. In the series analytic: Advances in molecular genetics of plant-microbe interactions. 2 / edited by E.W. Nester, and D.P.S. Verma. Proceedings of the 6th International Symposium on Molecular Plant-Microbe Interactions held July 1992, Seattle, Washington. Includes references.

Language: English

Descriptors: Medicago sativa; Structural genes; Naringenin-chalcone synthase; Oxidoreductases; Hydroxymethylglutaryl-coa reductase; Promoters; Dna binding proteins; Transcription; Gene expression; Genetic regulation; Phytoalexins; Biosynthesis

169 NAL Call. No.: QH426.M6 Transformation and foreign gene expression. Moloney, M.M.; Holbrook, L.A.
New York : Springer-Verlag; 1993.
Monographs on theoretical and applied genetics v. 19: p. 148-167; 1993. In the series analytic: Breeding oilseed brassicas / edited by K.S. Labana, S.S. Banga and S.K. Banga. Literature review. Includes references.

Language: English

Descriptors: Brassica napus; Brassica campestris; Brassica juncea; Genetic transformation; Agrobacterium tumefaciens; Plasmid vectors; Direct DNAuptake; Transgenic plants; Gene transfer; Genetic vectors; Cauliflower mosaic caulimovirus; Literature reviews; Gene expression

170 NAL Call. No.: SB249.N6 Transient expression of beta-glucuronidase gene in new hybrid of fine extra-long staple Egyptian cotton seedlings following biolistic particle bombardment.
Momtaz, O.A.; Madkour, M.A.
Memphis, Tenn. : National Cotton Council of America, 1991-; 1993. Proceedings / v. 2: p. 624-627; 1993. Meeting held on January 10-14, 1993, New Orleans, Louisiana. Includes references.

Language: English

Descriptors: Egypt; Cabt; Gossypium barbadense; Beta-glucuronidase; Hybrids; Direct DNAuptake; Genetic transformation; Gene expression

171 NAL Call. No.: QK710.P62 A tRNA Val(GAC) gene of chloroplast origin in sunflower mitochondria is not transcribed.
Ceci, L.R.; Saiardi, A.; Siculella, L.; Quagliariello, C. Dordrecht : Kluwer Academic Publishers; 1993 Nov. Plant molecular biology v. 23 (4): p. 727-736; 1993 Nov. Includes references.

Language: English

Descriptors: Helianthus annuus; Structural genes; Transfer RNA; Valine; Mitochondrial DNA; Gene expression; Transcription; Genomes; Chloroplasts; Mitochondrial genetics; Nucleotide sequences; Amino acid sequences; Chloroplast genetics; Repetitive DNA; Molecular conformation; Promoters

Abstract: A tRNA(Val) (GAC) gene is located in opposite orientation 552 nucleotides (nt) down-stream of the cytochrome oxidase subunit III (coxIII) gene in sunflower mitochondria. The comparison with the homologous chloroplast DNA revealed that the tRNA(Val) gene is part of a 417 nucleotides DNA insertion of chloroplast origin in the mitochondrial genome. No tRNA(Val) is encoded in monocot mitochondrial DNA (mtDNA), whereas two tRNA(Val) species are coded for by potato mtDNA. The mitochondrial genomes of different plant species thus seem to encode unique sets of tRNAs and must thus be competent in importing the missing differing sets of tRNAs.

172 NAL Call. No.: QK710.P62 Two classes of differentially regulated glutamine synthetase genes are expressed in the soybean nodule: a nodule-specific class and a constitutively expressed class.
Roche, D.; Temple, S.J.; Sengupta-Goplan, C. Dordrecht : Kluwer Academic Publishers; 1993 Sep. Plant molecular biology v. 22 (6): p. 971-983; 1993 Sep. Includes references.

Language: English

Descriptors: Glycine max; Multigene families; Complementary DNA; Glutamate-ammonia ligase; Nucleotide sequences; Amino acid sequences; Gene expression; Genetic regulation; Root nodules; Cotyledons; Plant tissues; Messenger RNA

Abstract: We have characterized two sets of cDNA clones representing the glutamine synthetase (GS) mRNA in soybean nodules. Using the 3'-untranslated regions of a representative member of each set, as gene member(s) specific probes, we have shown that one set of the GS genes are expressed in a nodule-specific manner, while the other set is expressed in other tissues, besides the nodules. The nodule-specific GS genes are expressed in a developmentally regulated manner in the nodules, independent of the onset of nitrogen fixation. The other class of GS genes is expressed constitutively in all tissues tested, but its expression level is dramatically enhanced in nodules following onset of N2 fixation. The latter set of genes is also expressed in cotyledons of germinating seedlings in a developmentally regulated manner. Analysis of hybrid select translation products and genomic Southern blots suggests that multiple gene members in each class are expressed in the nodules.

173 NAL Call. No.: 500 N21P Two functional soybean genes encoding p34cdc2 protein kinases are regulated by different plant developmental pathways. Miao, G.H.; Hong, Z.; Verma, D.P.S.
Washington, D.C. : The Academy; 1993 Feb01. Proceedings of the National Academy of Sciences of the United States of America v. 90 (3): p. 943-947; 1993 Feb01. Includes references.

Language: English

Descriptors: Glycine max; Amino acid sequences; Gene expression; Genetic code; Genetic regulation; Meristems; Nodules; Nucleotide sequences; Plant development; Protein kinase; Rhizobium; Saccharomyces cerevisiae

Abstract: We have isolated two cDNA clones (cdc2-S5 and cdc2-S6) encoding p34cdc2 protein kinases, homologs of yeast cdc2/CDC28 genes, from a soybean nodule cDNA library. The two sequences share 90% sequence homology in the coding regions. The 5' and 3' noncoding regions are distinct from each other, however, indicating that at least two genes encode p34cdc2 protein kinases in soybean. Both sequences can rescue the cdc28 mutation in Saccharomyces cerevisiae but rescue it with different efficiency. Genomic Southern analysis showed the existence of two copies for each of these genes, which are not closely linked and are nonallelic. The relative expression level of the two soybean p34cdc2 genes varies in different tissues. Expression of cdc2-S5 is higher in roots and root nodules, whereas cdc2-S6 is more actively expressed in aerial tissues, indicating that regulation of these two p34cdc2 gene.9 is coupled with plant developmental pathways. Expression of cdc2-S5 is, furthermore, enhanced after Rhizobium infection, whereas cdc2-S6 fails to respond, suggesting that cdc2-S5 plays a role in nodule initiation and organogenesis. This latter gene preferentially responds to auxin (alpha-naphthaleneacetic acid) treatment, indicating that phytohormones may be involved in the control of cell division mediated by Rhizobium infection. Thus, different p34cdc2 protein kinases may control cell division in different tissues in a multicellular organism and respond to different signals--e.g., phytohormones.

174 NAL Call. No.: 442.8 Z34 Use of the polymerase chain reaction to isolate an S-locus glycoprotein cDNA introgressed from Brassica campestris into B. napus ssp. oleifera. Goring, D.R.; Banks, P.; Beversdorf, W.D.; Rothstein, S.J. Berlin, W. Ger. : Springer International; 1992 Aug. M G G : Molecular and general genetics v. 234 (2): p. 185-192; 1992 Aug. Includes references.

Language: English

Descriptors: Brassica napus var. oleifera; Brassica campestris; Introgression; Structural genes; Dna; Glycoproteins; Loci; Self incompatibility; Nucleotide sequences; Gene expression; Alleles; Segregation; Polymerase chain reaction; Amino acid sequences; Inheritance

Abstract: A self-incompatible canola-quality Brassica napus ssp. oleifera line (W1) was generated by introgressing the S-locus from a self-incompatible B. campestris plant into the Westar cultivar. Using the polymerase chain reaction (PCR) with primers derived from conserved regions in S-locus glycoprotein (SLG) alleles, the central region of the active SLG gene (910) was obtained. The remaining portions of the cDNA for this 910 gene were subsequently cloned using the PCR-rapid amplification of cDNA ends (RACE) procedure. Sequence analysis revealed that the 910 cDNA show a high degree of sequence similarity to SLG alleles associated with Class I self-incompatible lines. The 910 gene was found to be absent in the original self-compatible cv. Westar (B. napus) and segregated with self-incompatibility in a mixed population generated from a cross between self-incompatible W1 and self-compatible Westar. RNA blot analysis indicated that high levels of 910 mRNAs were present in the stigma as buds approached anthesis. Thus, the SLG allele of W1 transferred from B. campestris via backcrosses to a line of cv. Westar has been identified.

175 NAL Call. No.: QH442.A1G4 Zea mI, the maize homolog of the allergen-encoding Lol pI gene of rye grass. Broadwater, A.H.; Rubinstein, A.L.; Chay, C.H.; Klapper, D.G.; Bedinger, P.A. Amsterdam : Elsevier Science Publishers; 1993. Gene v. 131 (2): p. 227-230; 1993. Includes references.

Language: English

Descriptors: Zea mays; Complementary DNA; Structural genes; Plant proteins; Nucleotide sequences; Amino acid sequences; Multigene families; Gene expression; Pollen; Immunohistochemistry; Comparisons; Allergens; Lolium perenne

Abstract: Sequence analysis of a pollen-specific cDNA from maize has identified a homolog (Zea mI) of the gene (Lol pI) encoding the major allergen of rye-grass pollen. The protein encoded by the partial cDNA sequence is 59.3% identical and 72.7% similar to the comparable region of the reported amino acid sequence of Lol pIA. Southern analysis indicates that this cDNA represents a member of a small multigene family in maize. Northern analysis shows expression only in pollen, not in vegetative or female floral tissues. The timing of expression is developmentally regulated, occurring at a low level prior to the first pollen mitosis and at a high level after this postmeiotic division. Western analysis detects a protein in maize pollen lysates using polyclonal antiserum and monoclonal antibodies directed against purified Lolium perenne allergen.

Abbott, L.K. 3
Ainley, W.M. 135
Allen, T. 146
Allison, L.A. 91
Almoguera, C. 52, 165
Altenbach, S.B. 2
Amasino, R.M. 28
Anderson, D.M. 33
Anderson, E.J. 24
Arahira, M. 35
Arias, J.A. 59
Axelos, M. 6
Axelrod, B. 43
Bagga, S. 45�
Baird, W.V. 61
Baker, M.E. 62
Bako, L. 7, 55
Bal, A.K. 139
Baltz, R. 27
Banks, P. 174
Banks, S.W. 11
Barker, D.G. 58, 137
Barz, W. 102
Bauer, P. 91
Baumlein, H. 36, 41, 161
Beachy, R.N. 72, 141
Bedinger, P.A. 175
Belanger, F. 134
Bergman, J.W. 10
Bernier, F. 101
Beversdorf, W.D. 174
Bewley, J.D. 46
Bhattacharyya, M.K. 168
Billy, F. de 137
Bisseling, T. 29, 31
Blank, C. de 31
Bogre, L. 7, 12, 19, 55, 119, 129
Boller, T. 32
Bonham-Smith, P.C. 50, 116
Bourque, J.E. 162
Boutry, M. 143
Bradley, D. 144
Brangeon, J. 77
Breda, C. 56, 127
Brenner, M.L. 135
Briquet, M. 143
Broadwater, A.H. 175
Broer, I. 88
Brown, D.C.W. 79
Brussel, A.N.A. van 4, 5
Buffard, D. 56, 127
Burkard, G. 54
Buzzell, R.I. 154
Caredda, S. 8
Carrayol, E. 120
Castonguay, Y. 78, 124, 125
Ceci, L.R. 171
Chamberland, S. 101
Chang, M.M. 111
Chang, Y.C. p34, 156
Chanut, F.A. 42
Chay, C.H. 175
Chen, T.H.H. 118
Cheon, C.I. 139
Chino, M. 64
Choudhary, A.D. 108
Christou, P. 131
Clark, D.C. 68
Clemens, J.C. 43
Clouse, S.D. 62
Coca, M.A. 165
Cocks, P.S. 8
Collins, G.B. 73
Covello, P.S. 149
Creelman, R.A. 47, 100
Crow, L.J. 81
Crowell, D.N. 28
Cullimore, J.V. 58
Cummins, I. 22
Curie, C. 6
Curry, J. 37
Czarnecka, E. 16
Daigle, N. 101
Dalkin, K. 108, 157
Datta, N. 120, 96
Davies, S.P. 87
Davis, L.C. 126
Day, D.A. 166
Dazzo, F.B. 158, 133
Dedeoglu, D. 7
Dedieu, A. 137
Deineko, E.V. 84
Delorme, R.M. 123
Deng, W. 73
DeWald, D.B. 47, 90
Dhindsa, R.S. 21, 39, 125, 148
Dhir, S. 134
Dhir, S.K. 134
Dickstein, R. 66
Didierjean, L. 54
Dietrich, R.A. 60
Dixon, J.E. 43
Dixon, R.A. 40, 59, 93, 108, 109, 110, 142, 157, 158, 168 Domon, C. 27
Dong, G. 148
Dong, J.L. 80
Donoho, G.P. 43
Dube, S. 112
Duc, G. 122, 143
Dudits, D. 7, 12, 55, 147
Dunn, K. 146
Dure L. III 145
Dwivedi, R.S. 155
Dyer, W.E. 10
Ebel, J. 115
Edwards, R. 108
El Turk, J. 127
Elthon, T.E. 166
Esnault, R. 56, 127
Estabrook, E. 92
Fahrendorf, T. 108, 158
Faktor, O. 40, 168
Falk, A. 85
Farmer, E.E. 136
Farnden, K.J.F. 94
Farrand, S.K. 134
Feder, A.I. 92
Fiedler, U. 41
Filistein, R. 41
Flamand, M.C. 143
Folk, W.R. 162
Fowler, T.J. 51
Franceschi, V.R. 1, 67
Franssen, H. 29, 31
Fruhling, M. 160
Fujiwara, T. 64, 72, 141
Fukazawa, C. 35
Ganter, G. 146
Gantt, J.S. 13, 113
Gartner, A. 12
Gee, M. 17
Gee, M.A. 70, 167
Geng, X.M. 79
Georgescu, A. 2
Gesteland, R.F. 42
Gidamis, A.B. 48, 63
Gijzen, M. 154
Glascock, C.B. 79, 75
Goblet, J.P. 143
Goldberg, R.B. 121
Goldmark, P.J. 37
Gonsalves, D. 38
Gordon, A.J. 23
Goring, D.R. 174
Gossett, D.R. 11
Gowri, G. 108
Grabau, E.A. 42
Grant, M.R. 94
Gray, M.W. 149
Grayburn, W.S. 73
Gregerson, R.G. 113
Grimes, H.D. 1, 67
Grula, J.W. 33
Guilfoyle, T.J. 14, 17, 70
Gulfoyle, T.J. 167
Gurley, W.B. 16
Gyorgyey, J. 12, 55
Hadwiger, L.A. 111
Hagen, G. 14, 17, 70, 167
Hamilton-Kemp, T.R. 73
Harada, J.J. 60
Harada, K. 83
Harrison, M.J. 93, 108, 109, 168
Harter, K. 102
Haser, A. 122
Hata, S. 119, 95
Heberle-Bors, E. 12, 19, 119, 129
Heim, U. 161
Hellyer, A. 97
Hendriks, P. 29
Herman, E. 112
Herman, E.M. 155
Hildebrand, D.F. 73
Hill, D.F. 94
Hill, J.W. 135
Hillemann, D. 88
Hilu, K. 61
Hirai, M.Y. 64
Hirel, B. 77, 120
Hirsch, A.M. 18, 82E
Hirt, H. 12, 19, 119, 129
Hitz, W.D. 1
Hoarau, A. 77
Hoarau, J. 77
Hobbs, S.L. 33
Holbrook, L.A. 169
Hong, Z. 159, 173
Horn, R. 107
Horovitz, D. 111
Howieson, J.G. 3, 8
Hu, C.A. 140
Hu, J.S. 38
Hu, W.H. 25
Hudspeth, R.L. 33
Huet, J.C. 26
Huiwen, Z. 79
Huystee, R.B. van 56
Ingersoll, J.C. 16
Inze, D. 36
Itoh, Y. E35
Iwamoto, H. 152
James, C.L. 23
John, M.E. 28, 81
Johnson, R.R. 136
Johnson, W.B. 105
Johnson-Flanagan, A.M. 79
Jonak, C. 12, 119, 129
Jordano, J. 52, 165
Journet, E.P. 137
Junghans, H. 157
Kalinski, A. 112, 155
Kammen, A. van 29
Kamoun, S. 79, 75
Kanamori, J. 63
Kandasamy, M.K. 71
Kang, I.J. 63
Kapazoglou, A. 145
Kapros, T. 7, 55, 147
Katinakis, P. 29, 31
Kato, T. 15, 20, 152
Kawamura, Y. 20
Kawasaki, T. 20
Kearns, A. 166
Keddie, J.S. 68
Kemp, J.D. 45
Kennedy, R.A. 44
Key, J.L. 120, 96, 128, 135
Kijne, J.W. 4, 5
Kikuchi, A. 83
Kiss, G.B. 91
Kitamura, K. 83
Kitamura, Y. 35
Kito, M. 48, 63
Klapper, D.G. 175
Knauf, V.C. 105
Knight, T.J. 106
Knox, R.B. 87
Knutzon, D.S. 105
Komarova, M.L. 84
Komeda, Y. 64
Kondorosi, A. 91, 127
Kondorosi, E. 91
Kouchi, H. 119, 95
Kridl, J.C. 105
Kriz, A.L. 134
Krochko, J.E. 46R
Kroner, P.A. 120, 96
Kuo, C.C. 2
Kuster, H. 160
Kwan, B.Y.H. 87
Laberge, S. 78, 124, 125
LaCelle, M.G. 11
LaFayette, P.R. 120, 96
Lam, E. 86
Lamb, C.J. 40, 59, 108, 168
Langis, R. 21
Langner, C.A. 61
Larsen, K. 58
Lauridsen, P. 104
Laursen, N.B. 150
Leaver, C.J. 49
Lee, N.G. 139
Lee, S.P. 118
Lenman, M. 85
Lescure, B. 6
Lessard, P.A. 141
Li, J.L. 80
Li, M. 68
Li, N. 112
Li, Y. 14, 17, 70, 167
Liboz, T. 6
Lin, J.J. 44
Lingle, W.L. 135
Liu, D. 112
Liu, Z. 17
Loader, N.M. 97
Loake, G.J. 40, 108, 168
Lobler, M. 18, 82
Loi, A. 8
Lough, T.J. 94
Lucas, M.C. 11
Lugtenbergh, B.J.J. 4, 5
Maccarrone, M. 164
Machlin, S. 144
Machmudova, A. I99
Madkour, M.A. 170
Madsen, O. 151
Magyar, Z. 7, 147
Mairinger, T. 119
Marcker, K.A. 104, 150, 151
Margis-Pinheiro, M. 54
Markley, N.A. 116
Marsolier, M.C. 77, 120
Martin, C. 54
Martin, G. 70, 167
Mason, H.S. 47, 90
Mattoo, A.K. 112
Maxwell, C.A. 108, 109
McCabe, D.E. 131
McHughen, A. 9
McKhann, H.I. 18
McMorris, T.C. 62
McNeil, K.J. 135
Mellor, R.B. 32
Melroy, D.L. 155
Meskiene, I. 19, 119
Miao, G.H. 153, 159, 173
Mikami, B. 48
Milhollon, E.P. 11
Miller, S.S. 13, 113
Mink, M. 12
Mitchell-Olds, T. 144
Moloney, M.M. 50, 116, 169
Momtaz, O.A. 170
Moneger, F. 49
Monroy, A. 148
Monroy, A.F. 39, 125
Montane, M.H. 6
Morris, C.F. 37
Mujer, C.V. 44
Muller, J. 32
Mullet, J.E. 47, 90, 100
Mur, L.A. 4, 5
Murphy, D.J. 22, 68
Mylona, P. 31
Nadeau, P. 78
Nagao, R.T. 120, 96, 128, 135
Nagpala, P.G. 38
Nagy, I. 36
Naito, S. 64
Narvaez-Vasquez, J. 53
Nasrallah, J.B. 71, 130
Nasrallah, M.E. 71, 130
Nemeth, K. 55
Ngo, W. 66
Ni, W. 168
Nishio, T. 71
Nugent, J.M. 30
Nykiforuk, C.L. 79
O'Brian, M.R. 74
O'Brien, A.P. 87
Oancia, T.L. 50
Ocsovszky, I. 147
Ohta, H. 15
Okamuro, J.K. 121
Okubo, K. 83
Oommen, A. 168
Orozco-Cardenas, M.L. 53
Ougham, H.J. 23
Overvoorde, P.J. 1
Paiva, N. 168
Palmer, J.D. 30
Pang, S.Z. 38
Paolillo, D.J. 71
Parthier, B. 99
Pathirana, S.M. 13
Pay, A. 19, 119, 129
Pearson, K.W. 2
Peng, T. 66
Perlick, A.M. 160, 163
Pernollet, J.C. 26
Pfosser, M. 12
Pichon, M. 137
Pierre, M. 91
Pillay, D.T.N. 27
Pladys, D. 132
Poiret, M. 91
Potenza, C. 92
Pramanik, S.K. 46
Prusty, R. 66
Puhler, A. 88, 160, 163
Quagliariello, C. 138, 171
Radke, S.E. 60, 105
Ragland, M. 76
Raja, S. 146
Ramiov, K.B. 150
Rask, L. 85
Recourt, K.� 4, 5
Reddington, B.D. 94
Reinbothe, C. 99
Reinbothe, S. 99
Reviron, M.P. 26
Reynolds, P.H.S. 94
Ricardo, C.P. 117
Ripp, K. 1
Rivkin, M.I. 84
Robinson, D.L. 122
Robinson, S.J. 98
Robson, A.D. 3
Roche, D. 172
Rodrigues-Pousada, C. 117
Romero, L.C. 86
Rothstein, S.J. 174
Rouan, D. 6
Rubinstein, A.L. 175
Rumpho, M.E. 44
Russell, D. 28
Ryan, C.A. 53, 136
Safford, R. 97, 98
Sagliocco, F. 145
Saiardi, A. 138, 171
Sakai, F. 80
Sallantin, M. 26
Sallaud, C. 127
Salzwedel, J.L. 158, 133
Sandal, L. 151
Sandal, N.N. 151
Sangwan, I. 74
Sarhan, F. 39, 125
Sato, T. 71
Savka, M.A. 134
Savoure, A. 91
Schafer, E. 102
Schafer, R. 77
Schoelz, J.E. 24
Schroder, J. 69
Sehgal, O.P. 24
Sengupta-Gopalan, C. 45, 92, 106
Sengupta-Goplan, C. 172
She, Q. 104
Shen, B. 126
Shen, S.C. 25
Shen, W. 25
Shibata, D. 15, 20, 152
Shirano, Y. 152
Shorrosh, B.S. 110, 142
Shumnyi, A.V.K. 84
Siculella, L. 171
Siddique, A.B.M. 139
Siemieniak, D.R. 38
Silva, J. de 98
Simpson, R.B. 135
Singh, J. 79
Singh, M. 87
Skorupska, H.T. 123
Slabas, A.R. 97
Slightom, J.L. 38
Slocum, R.D. 114
Smart, C.J. 49
Smith, L.J. 68
Smith, M.E. 66
Smolders, A. 29
Spee, J. 29
Staehelin, C. 32
Stanford, A.C. 58
Staraci, L.C. 2
Steczko, J. 43
Stefanov, I. 147
Steinmetz, A. 27
Stermer, B. 168
Stougaard, J. 104, 150
Strabala, T. 17
Sugimoto, T. 20�
Sutton, D. 45
Suzuki, H. 51, 57
Szalay, A. 119
Szoke, A. 159
Talke-Messerer, C. 102
Tanaka, K. 15
Taylor, M.G. 65
Temple, S.J. 106, 172
Theil, E.C. 76
Thiele, D.J. 103
Thompson, G.A. 105
Tierney, M.L. 51, 57, 100
Toriyama, K. 71
Townsend, J. 2
Tranbarger, T.J. 67
Trese, A.T. 24
Truchet, G. 137
Tsukamoto, C. 83
Tunen, A.J. van 4, 5
Twary, S.N. 113
Tyler, B.M. 79, 75
Tyson, H. 21
Uhlmann, A. 115
Ulmasov, T. 17
Ulmasov, T.N. 70, 167
Unkefer, P.J. 106
Utsumi, S. 48, 63
Van Huystee, R. 154
Vance, C.P. 13, 113, 122, 132
Vartanian, N. 26
Vasil, I.K. 65
Vasil, V. 65
Vassilevskaia, T.D. 117
Veldink, G.A. 164
Verma, D.P.S. 77, 139, 140, 153, 159, 173 Vershinin, A.V. '84
Vezina, L.P. 124, 125
Vienne, D. de 26
Villarroel, R. 36
Vliegenthart, J.F.G. 164
Vries, F. de 29
Wagner, T. 57
Wainwright, C. 2
Walker-Simmons, M.K. 37
Walling, L.L. 34, 156
Walter, C. 88
Warkentin, T.D. 9
Wasternack, C. 99
Waterborg, J.H. 89
Weber, H. 161
Welle, R. 69
Werth, C.R. 61
Whelan, J. 166
Whittier, R.F. 20
Widholm, J.M. 134
Wiemken, A. 32
Williamson, C.L. 114
Wobus, U. 36, 41, 161
Wolfraim, L. 148
Wolfraim, L.A. 21
Woolner, E.M. 97
Wu, S.C. 55
Wyatt, R.E. 128
Xu, H. 87
Xu, X.L. 25, 80
Xue, J. 85
Xue, Z.T. 25
Yang, W.C. 29, 31
Ying, M.C. 10
Young, M. 79, 75
Young, S. 166
Zetsche, K. 107
Zhang, M. 140
Zhuang, N.L. 25
Zurek, D.M. 62 2,4-d 7, 57, 62
Abiotic injuries 28, 57, 90, 157
Abscisic acid 37, 52, 79, 118
Acc 112
Acclimatization 21, 39, 118, 124
Acetylene reduction 122
Acid phosphatase 90
Acidity 3
Active transport 1
Acyltransferases 88, 135
Adaptation 8, 26
Aerobic treatment 44
Agrobacterium 11, 72
Agrobacterium rhizogenes 51
Agrobacterium tumefaciens 9, 10, 14, 16, 18, 35, 45, 51, 71, 84, 98, 101,
135, 169
Albumins 2
Alcohol dehydrogenase 16
Alcohol oxidoreductases 118
Alfalfa mosaic virus 54
Alleles 61, 121, 123, 154, 174
Allergens 175
Amino acid sequences 1, 12, 13, 15, 17, 19-22, 25-28, 30, 31, 33, 37, 38,
42, 43, 50, 54, 66, 74, 81, 82, 85, 87, 91, 94-97, 109-120, 124, 125, 127, 129, 137, 139, 142, 144, 145, 149, 151-153, 157, 158,
160, 161, 171-175
Amino acids 2, 67
Aminotransferases 74
Ammonia 77, 120
Anaerobic conditions 44
Anthers 87
Antigens 116
Antisense DNA 162
Antisense RNA 106, 139, 141
Apical meristems 50
Arabidopsis 17
Arabidopsis thaliana 6, 85, 87
Arachis hypogaea 56
Asparaginase 94
Aspartate-ammonia ligase 163
Auxins 17, 70, 120, 96, 112, 120, 96, 167 Bacterial proteins 4, 5
Bacteroids 113, 122, 140
Bertholletia excelsa 2
Beta-glucan 115
Beta-glucanase 111
Beta-glucuronidase 9, 10, 11, 14, 17, 33, 35, 41, 51, 60, 65, 72, 80, 87,
90, 98, 101, 104, 131, 141, 147, 170
Binding proteins 1, 86, 139
Binding site 16, 27, 35, 43
Biochemical pathways 108
Biochemical polymorphism 83
Biosynthesis 4, 5, 69, 93, 105, 108, 159, 161, 168 Bradyrhizobium 166
Bradyrhizobium japonicum 31, 32, 92, 95, 119, 126, 139, 166 Brassica campestris 6, 30, 71, 75, 79, 87, 105, 130, 144, 169, 174

Brassica campestris var. rapa 24
Brassica juncea 169
Brassica napus 2, 50, 60, 71, 79, 85, 97, 98, 102, 105, 116, 130, 169
Brassica napus var. oleifera 26, 174 Brassica oleracea 71, 130
Brassinolide 62
Bromus inermis 118
Bromus secalinus 37
Buds 10, 12, 50
Cabt 170
Calcium 3
Calcium ions 39
Callus 7, 10, 88, 134
Carboxylic acids 159
Carthamus tinctorius 10
Cauliflower mosaic caulimovirus 24, 45, 53, 169 Cell differentiation 18, 60, 92, 119, 95, 119, 95, 122, 139, 140

Cell division 7, 12, 19, 29, 147
Cell growth 55
Cell membranes 139
Cell suspensions 7, 21, 39, 56, 65, 88, 102, 118, 119, 157, 158 Cell ultrastructure 71
Cell wall components 51, 57, 75, 79 100, 115, 128, 157 Cellular biology 100
Chalcone isomerase 92, 127
Chemical composition 159
Chemical reactions 16, 89
Chimeras 2, 24, 131
Chitinase 32, 54
Chitosan 111
Chlamydomonas reinhardtii 103
Chloramphenicol acetyltransferase 104, 162 Chlorophyll a/b binding protein 33, 34, 102, 145, 156 Chloroplast genetics 171
Chloroplasts 123, 171
Chromatin 89
Clones 55, 129
Cloning 37, 38, 43, 50, 54, 69, 81, 118, 152, 158 Coat proteins 38
Cold 21, 39, 78, 118, 125
Cold hardening 78, 125
Cold shock 164
Cold stress 124, 164
Cold tolerance 78, 148
Comparisons 175
Complementary DNA 19, 21, 27, 31, 54, 66, 74, 87, 95-97, 106, 113-120, 124, 125, 127, 139, 151, 153, 157, 160, 163, 172, 175

Complementation 19
Controlling elements 6, 60, 101, 121 Cortex 32, 60
Cotyledons 1, 15, 34, 99, 128, 145, 156, 172 Crops 75, 79
Crystallization 48
Crystals 48
Cultivars 25, 78, 123, 154
Culture media 10
Cysteine 63, 132
Cytochrome p-450 158
Cytochrome-c oxidase 138, 149
Cytokinins 14, 17
Cytoplasm 77
Cytoplasmic male sterility 49, 107, 143 Cytosol 77
Dark 23
Daucus carota 162
Defense mechanisms 54, 111, 115, 127 Deletions 35, 41, 51, 63, 90, 104
Derivatives 90, 136
Desiccation 79
Developmental stages 29, 131, 156
Diploidy 61
Direct DNAuptake 65, 169, 170
Disease resistance 32, 75, 79, 111, 127 Dna 1, 12, 13, 20, 24, 36, 52, 69, 94, 110, 111, 129, 142, 143, 174
Dna binding proteins 6, 16, 27, 35, 168 Dna libraries 81, 163
Dna polymerase 116
Dna replication 116
Dna sequencing 38
Drought 26, 124
Dwarfing 24
Echinochloa 44
Echinochloa crus-galli 44
Echinochloa crus-pavonis 44
Echinochloa muricata 44
Echinochloa oryzoides� 44
Edaphic factors 8
Egypt 170
Electrophoresis 123
Eleusine 61
Embryogenesis 34, 35, 52, 60, 99, 121 Environmental factors 8
Enzyme activity 4, 5, 7, 11, 13, 23, 43, 56, 67, 69, 72-74, 76, 88,
106, 108, 113, 120, 122, 131-133, 141, 154, 158, 159, 162, 164, 166

Enzyme inhibitors 39, 136
Enzyme polymorphism 123
Enzyme precursors 97
Enzymes 122
Epicotyls 62
Epidermis 51, 119, 95, 119, 95, 128, 137 Escherichia coli 3, 14, 48, 63, 68, 159 Ethylene 56, 112
Etiolation 74
Evolution 6, 149
Exons 25, 45, 153
Explants 10
Extracts 9
Fatty acids 73
Ferritin 76
Flavonoids 4, 5, 93, 108
Flowering 119
Flowers 12, 50, 53, 117, 157
Freezing 39, 78, 118, 125
Frost 79
Fructose 47
Fungal diseases 111, 157
Fusarium solani f.sp. phaseoli 111
Fusarium solani f.sp. pisi 111
Gelation 63
Gels 63
Gene expression 1-69, 71-175
Gene transfer 2, 11, 53, 63, 64, 68, 120, 134, 159, 169 Genes 2, 3, 14, 24, 38, 56, 62, 71, 72, 98, 120, 145, 146 Genetic analysis 24, 61, 129
Genetic change 123
Genetic code 11, 15, 29, 58, 61, 82, 94, 109, 112, 129, 152, 156, 161, 165,
173
Genetic engineering 69, 105
Genetic improvement 131
Genetic markers 131
Genetic polymorphism 83
Genetic regulation 3, 7, 13, 15, 16, 21, 29, 31, 34-37, 40, 41, 44,
46, 51, 52, 54, 55, 59-62, 64, 67, 71, 75, 77, 79, 88, 90, 92, 96, 98, 99, 101, 103, 104, 106, 108, 111, 113-115, 118, 120, 121, 124, 125, 132, 135, 137, 139, 141, 154, 157, 159, 161, 164, 166-168,
172, 173
Genetic transformation 2, 6, 9-11, 14, 16, 18, 35, 41, 45, 51, 53, 60,
63, 65, 71, 72, 77, 80, 84, 87, 88, 90, 98, 101, 104, 106, 121, 131, 134, 135,
137, 139, 141, 147, 150, 153, 159, 169, 170 Genetic variation 61, 123, 132, 154
Genetic vectors 169
Genome analysis 138
Genomes 171
Genotypes 8, 132, 154
Germ line 131
Globulins 35, 48
Glomus versiforme 93
Glucose 47
Glufosinate 88
Glutamate-ammonia ligase 23, 77, 106, 113, 120, 172 Glyceraldehyde-3-phosphate dehydrogenase 123 Glycine 78
Glycine max 1, 15-17, 20, 23, 25, 28, 29, 31, 32, 34, 35, 42, 43, 47,
48, 51, 57, 59, 62-64, 67, 69, 70, 72-74, 76, 77, 80, 83, 86, 90, 92,
95, 96, 100, 101, 103, 104, 112, 115, 119-121, 123, 126, 128, 131, 134, 135, 139, 149-156, 159, 162, 164, 166, 167, 172,
173
Glycine tomentella 126
Glycoproteins 71, 130, 155, 174
Glycyrrhiza glabra 80
Gossypium barbadense 170
Gossypium hirsutum 33, 81, 99, 145
Greening 114
Growth 8, 102
Growth promoters 40
Guanine 86
Guanosine triphosphate 139
Healing 112
Heat 88
Heat shock 52, 135, 164
Heat shock proteins 16, 52, 135, 165 Heat stress 164
Helianthus annuus 16, 22, 27, 49, 52, 68, 107, 138, 165, 171 Herbicide resistance 88
Hibiscus cannabinus 11
Histidine 43
Histochemistry 14, 120, 154
Histoenzymology 33, 41, 51, 80, 87, 90, 98, 101, 104, 147 Histones 7, 55, 89, 147
Homologous recombination 42
Hordeum vulgare 99
Hybrids 126, 170
Hydro-lyases 108
Hydroxymethylglutaryl-coa reductase 168 Hypocotyls 57, 100, 128
Iaa 57
Imbibition 37
Immunoblotting 53
Immunochemistry 116
Immunocytochemistry 71, 77
Immunohistochemistry 175
In vitro 38, 59
In vitro culture 9
Induced mutations 63, 101
Induced resistance 75, 79
Induction 44, 99, 136
Infection p4, 5
Infections 54
Inheritance 83, 123, 174
Injuries 47, 56, 100
Interspecific hybridization 126
Introgression 174
Introns 6, 25, 27, 45, 144, 145, 149, 153 Inversion 107
Iron p76
Isocitrate dehydrogenase 61, 110
Isoenzymes 61, 115, 164
Isoflavones 93
Isomerases 142
Isopentenyladenosine 135
Jasmonic acid 47, 90, 99, 100, 136, 152 Kinases 129
Laboratory methods 10
Leaves 12, 20, 26, 28, 33, 45, 50, 53, 54, 56, 57, 74, 77, 101, 114, 117,
119, 127, 128, 145, 151, 152, 157, 159 Lectins 121
Leghemoglobin 23, 76, 104, 132, 146, 150, 163 Legumin 36
Leguminosae 75, 79, 140
Length 62
Lens culinaris 9
Life cycle 67
Ligases 45, 108, 115
Light 120, 96, 102, 120, 96
Line differences 123
Lines 123
Linkage 123
Linkage groups 123p
Lipid bodies 68
Lipid metabolism 73, 105
Lipogenesis 98
Lipoxygenase 15, 43, 67, 73, 152, 163, 164 Literature reviews 108, 130, 169
Loci 42, 123, 130, 174
Lolium perenne 175
Lotus corniculatus 104, 120, 150, 153 Lupinus albus 117
Lupinus arboreus 94
Lyases 112
Lycopersicon esculentum 6, 53, 136
Macroptilium atropurpureum 166
Medicago 3, 157
Medicago falcata 21
Medicago littoralis 3
Medicago polymorpha 3, 8
Medicago sativa 7, 12, 13, 18, 19, 39, 40, 45, 46, 53, 55, 66, 78, 82, 84,
88, 91, 93, 106, 108, 109, 110, 113, 119, 124, 125, 127, 129, 132, 136, 142,
146, 147, 148, 158, 168
Medicago truncatula 3, 58, 93, 137
Medicago varia 12, 89, 129, 147
Medicarpin 93
Mercuric chloride 54
Meristems 18, 173
Mesophyll 1, 7
Messenger RNA 1, 4, 5, 7, 12, 13, 17, 19, 20-23, 25-27, 33, 34, 37, 39, 42, 46, 47, 50-55, 57, 62, 66, 67, 74, 76-78, 81, 85, 92-97, 99, 106, 110, 111, 113-120, 122, 124, 125, 127, 128, 136,
138, 139, 141-145, 151, 153, 156, 157, 160, 163-165, 167, 172 Metabolic inhibitors 39
Metabolism 161
Metal ions 103
Methionine 2, 64, 162
Mice 103
Microtubules 129
Mitochondria 138, 166
Mitochondrial DNA 30, 42, 49, 107, 143, 149, 171 Mitochondrial genetics 42, 49, 107, 149, 171 Molecular biology 24, 109
Molecular conformation 25, 48, 68, 171 Molecular genetics 105, 112
Molecular mapping 49, 59, 107
Multigene families 6, 13, 16, 25, 27, 28, 31, 34, 45, 50, 51, 57, 59, 85,
87, 91, 96, 97, 110, 115, 117, 119, 120, 124, 128, 130, 144, 153, 157,
167, 172, 175
Multiple genes 42, 77
Mutagenesis 150
Mutants 18, 19, 66, 101, 122
Mutations 6, 43, 121, 122
Naa 7, 57
Nadh 113
Nadh dehydrogenase 30
Nadp 123
Naringenin-chalcone synthase 4, 5, 40, 59, 69, 75, 79, 92, 93, 127,
157, 168
Nicotiana 101
Nicotiana tabacum 6, 14, 35, 36, 41, 51, 53, 59, 70, 72, 73, 75, 77, 79,
87, 90, 98, 106, 121, 135, 136, 141, 147, 153, 159 Nitrogen 67
Nitrogen fixation 18, 113, 122, 126, 146 Nitrogenase 76
Nodulation 3, 4, 5, 8, 18, 31, 66, 76, 91, 92, 109, 122, 126, 133, 137, 139, 140, 146, 158, 133
Nodules 173
Nodulins 31, 66, 82, 91, 95, 119, 122, 126, 132, 137, 140, 146, 153, 163
Nuclei 143, 149
Nucleic acids 58
Nucleotide sequences 1, 6, 12, 13, 16, 19-22, 25, 27-31, 33, 36-38, 40, 42, 50, 52, 54, 66, 74, 77, 81, 82, 85, 87, 90, 91, 94-98,
101, 108-120, 124, 125, 127, 129, 137-139, 142-145, 149-153, 157, 158, 160, 161, 171-175
Nucleotides 86
Nutrient availability 67
Nutrient deficiencies 67
Nutrient requirements 64
Ontogeny 29
Organelles 155
Organogenesis 135
Oryza sativa 44
Osmoregulation 114
Osmotic pressure 52, 114
Oxidoreductases 69, 93, 114, 127, 151, 159, 166, 168 Ozone 164
P-coumaric acidp 40
Panicum maximum 65
Pathogenesis-related proteins 127
Pedigree 123
Pennisetum Americanum 65
Pennisetum purpureum 65
Peroxidase 32, 56, 133, 154, 158
Peroxidases 133, 158
Peroxidation 73
Petioles 119
Petunia 64
Ph 3, 132
Phanerochaete chrysosporium 103
Phaseolin 45
Phaseolus vulgaris 40, 45, 54, 59
Phenotypes 24, 61, 131
Phenylalanine ammonia-lyase 4, 5, 92, 93 Phloem 128
Phloem companion cells 1
Phoma medicaginis 157
Phosphoenolpyruvate carboxylase 13, 20, 132 Phosphogluconate dehydrogenase 61
Phosphoproteins 39
Phosphorylation 7, 39
Phosphotransferases 45
Photosynthesis 47
Photosystem ii 145
Phytoalexins 69, 158, 168
Phytochrome 86
Phytophthora cryptogea 75, 79
Phytophthora megasperma 115
Phytophthora nicotianae var. parasitica 75, 79 Pisum sativum 29, 111, 114, 133, 158 Plant 90, 133, 158
Plant anatomy 29, 120, 131, 154, 156 Plant breeding 108
Plant composition 15, 32, 61, 67, 132, 154, 161 Plant development 14, 17, 34, 58, 96, 110, 120, 123, 132, 142, 173

Plant embryos 22, 35, 37, 46, 52, 60, 73, 79, 97, 99, 101, 119 Plant morphology 14, 120, 131
Plant organs 14
Plant pathogens 32
Plant physiology 17
Plant proteins 1, 2, 12, 21, 22, 25, 26, 28, 39, 41, 42, 46, 51, 52, 57,
63,
68, 72, 79, 87, 96, 98-101, 116, 118, 120, 124, 125, 128, 129, 139, 141, 152, 163, 167, 175
Plant tissues 14, 152, 172
Plants 30
Plasma membranes 1
Plasmid vectors 65, 169
Plasmids 3, 84, 133, 143, 158
Pods 111, 152
Pollen 27, 87, 130, 175
Pollen tubes 130
Polymerase chain reaction 174
Precursors 48, 63, 155
Proline 57, 82, 100, 128, 159
Promoters 6, 14, 16, 33, 35, 36, 41, 45, 51, 53, 59, 65, 75, 79 80, 87, 90, 98, 101, 104, 120, 121, 135, 141, 147, 150, 153, 167, 168,
171
Propionic acid 108
Protein composition 132
Protein content 67
Protein kinase 7, 19, 39, 119, 130, 173 Protein synthesis 36, 44, 46, 47, 64, 67, 71, 78, 89, 99, 109, 122, 136,
155, 161, 165, 166
Protein value 2
Proteinase inhibitors 53
Proteinases D132, 136, 155
Proteins 6, 50, 79, 75, 79, 75
Proteolysis 132
Protoplasts 7, 38, 102, 134
Pseudogenes 42
Pseudomonas syringae pv. pisi 127
Purification 69
Rapeseed oil 105
Raphanus sativus 75, 79
Rats 103
Recessive genes 122
Recombinant DNA 18, 33, 35, 45, 48, 53, 60, 65, 68, 80, 87, 90, 104, 135,
141, 147, 162
Regenerative ability 10, 11, 88, 134 Regulation 39, 47, 78, 79, 120, 136, 162 Repetitive DNA 25, 42, 171
Reporter genes 10, 14, 33, 35, 41, 45, 51, 60, 65, 72, 80, 87, 90, 98, 101,
104, 141, 147, 162
Respiration 166
Responses 165
Restriction mapping 25, 42, 49, 137
Rhizobium 31, 122, 140, 173
Rhizobium fredii 126
Rhizobium leguminosarum 3, 4, 5, 158, 133, 158, 133 Rhizobium meliloti 3, 8, 18, 66, 82, 109, 113, 137 Rhizobium trifolii 158, 133, 158, 133 Ribosomes 50
Ribulose-bisphosphate carboxylase 34 Rna 24, 162
Rna editing 30, 149
Rna polymerase 162
Root exudates 3
Root hairs 18, 92, 158, 133, 158, 133 Root meristems 60, 153
Root nodules 3, 13, 18, 23, 29, 32, 45, 66, 74, 76, 77, 82, 91, 92, 119,
95,
104, 113, 119, 95, 122, 132, 137, 139, 140, 146, 151, 153, 157, 159, 160, 163,
166, 172
Roots 4, 5, 7, 12, 18, 20, 28, 29, 32, 34, 45, 51, 56, 57, 60, 77, 92, 93,
95, 101, 104, 109, 111, 114, 117, 119, 127, 133, 137, 153, 154, 157-159,
166
Saccharomyces cerevisiae 19, 103, 173 Saccharum officinarum 65
Salinity 26, 114
Sardinia 8
Saturated fatty acids 105
Seed development 2, 46, 79, 94, 98, 161 Seed dormancy 37
Seed germination 15, 79
Seed maturation 155
Seedling growth 62
Seedlings 28, 52, 57, 60, 114, 156, 164 Seeds 2, 20, 22, 35, 36, 37, 41, 45, 48, 52, 64, 72, 83, 97, 98, 101, 128,
141, 155
Segregation 174
Self compatibility 71
Self incompatibility 71, 130, 174
Senescence 28, 132
Shoot meristems 147
Shoots 10, 135, 166
Sinapis alba 85
Sodium chloride 114
Soil acidity 8
Solanaceae 75, 79
Solanum nigrum 53
Somatic embryogenesis 46, 55
Southern blotting 143
Spatial distribution 71, 95, 119, 156 Squash mosaic comovirus 38
Stability 24
Starch 161
Stems 12, 20, 33, 34, 45, 56, 95, 111, 119, 157 Stigma 130
Strain differences 24
Strains 24
Stress 8, 23, 28, 52, 158
Stress response 44, 56, 78
Structural genes 1, 7, 12, 13, 16, 19-22, 27, 30, 33-35, 41, 42, 45, 51-54, 57, 60, 66, 74, 77, 87-89, 91, 92, 94, 106, 107, 110, 111, 114, 117, 119, 121, 125, 135, 137, 140, 142, 144, 149, 151, 153,
157, 160, 164, 167, 168, 171, 174, 175 Structure 83
Sucrose 1, 47, 90, 102
Sucrose synthase 23, 160, 161, 163
Sulfhydryl groups 63
Sulfur 64
Symbiosis 3, 32, 132, 146
Symptoms 24
Synergism 24
Targeted mutagenesis 63
Testas 128, 154
Thioglucosidase 85, 144
Thiolester hydrolases 97
Thiols 155
Tissue culture 11
Tobacco 38
Tolerance 3, 39, 118, 125
Torulopsis glabrata 103
Toxins 86
Transcription 3, 6, 7, 16, 17, 30, 34, 41, 42, 49, 55, 56, 59, 62, 79, 82,
86, 89, 94, 96, 99, 101, 103, 106-109, 120, 121, 129, 137, 138, 143, 149, 162-164, 168, 171
Transduction 148
Transfer RNA 162, 171
Transferases 4, 5, 108
Transformation 69
Transgenic plants 35, 41, 65, 72, 87, 90, 104, 131, 135, 139, 147, 153,
169
Transgenics 2, 6, 14, 45, 51, 53, 60, 64, 70, 71, 73, 77, 81, 84, 88, 98,
101, 106, 120, 121, 134, 137, 141, 159 Translation 6, 78, 106, 164
Transposable elements 25
Trifolium repens 133, 158
Triterpenoid saponins 83
Triticum aestivum 65
Tubulin 117
Ubiquitin 65
Ultraviolet radiation 16, 54
Vacuoles 53
Valine 171
Vesicular arbuscular mycorrhizas 93
Vicia faba 36, 41, 122, 143, 160, 161, 163 Vicia sativa subsp. nigra 4, 5
Vigna aconitifolia 51, 139
Viral antigens 24
Virulence 24
Water deficit 26
Water stress 26, 124, 165
X ray diffraction 48
Xanthomonas campestris pv. alfalfae 127 Xanthomonas campestris pv. armoraciae 75, 79 Xylem 128
Zea mays 6, 16, 65, 175
Zeatin riboside 7
Zinc 27
Zygotes 46 BULLET 15

ELECTRONIC MAIL ACCESS FOR INTERLIBRARY LOAN (ILL) REQUESTS

June 1993

The National Agricultural Library (NAL), Document Delivery Services Branch accepts ILL requests from libraries via several electronic services. All requests must comply with established routing and referral policies and procedures. The transmitting library will pay all fees incurred during the creation of requests and communication with NAL. A sample format for ILL requests is printed below along with a list of the required data/format elements.

ELECTRONIC MAIL - (Sample form below)

     SYSTEM            ADDRESS CODE
     ====================================================
     INTERNET. . . . . LENDING@NALUSDA.GOV
     EASYLINK. . . . . 62031265
     ONTYME. . . . . . NAL/LB
     TWX/TELEX . . . . Number is 710-828-0506 NAL LEND.
                       This number may only be used for
                       ILL requests.
     FTS2000 . . . . . A12NALLEND 
     OCLC  . . . . . . NAL's symbol AGL need only be entered
                       once, but it must be the last entry in
                       the Lender string.  Requests from USDA
                       and Federal libraries may contain AGL
                       anywhere in the Lender String.

SAMPLE ELECTRONIC MAIL REQUEST

| AG University/NAL    ILLRQ 231     4/1/93     NEED BY:  6/1/93 |
|                                                                |
| Interlibrary Loan Department                                   |
| Agriculture University                                         |
| Heartland, IA  56789                                           |
|                                                                |
| Dr. Smith   Faculty   Ag School                                |
|                                                                |
| Canadian Journal of Soil Science 1988 v 68(1):  17-27          |
| DeJong, R.  Comparison of two soil-water models under          |
| semi-arid growing conditions                                   |
| Ver:  AGRICOLA                                                 |
| Remarks:  Not available at IU or in region.                    |
| NAL CA:  56.8 C162                                             |
|                                                                |
| Auth:  C. Johnson      CCL     Maxcost: $15.00                 |
|                                                                |
| MORE                                                           |
|                                                                |

TELEFACSIMILE - Telephone number is 301-504-5675. NAL accepts ILL requests via telefacsimile. Requests should be created on standard ILL forms and then faxed to NAL. NAL does not fill requests via Fax at this time.

REQUIRED DATA ELEMENTS/FORMAT

Borrower's address must be in block format with at least two blank
lines above and below so form may be used in window envelopes.
Provide complete citation including verification, etc.
Provide authorizing official's name (request will be rejected if
not included).
Include statement of copyright compliance if applicable.
Indicate willingness to pay applicable charges.
Include NAL call number if available.Contact the Document Delivery
Services Branch at (301) 504-6503 if additional information is required.

NAL DOCUMENT DELIVERY SERVICES

June 1993

United States Department of Agriculture National Agricultural Library
Public Services Division
Document Delivery Services Branch
Beltsville, Maryland 20705-2351

The National Agricultural Library has established document delivery service policies for three user categories. They are 1) individuals; 2) libraries, other information centers, and commercial organizations; and 3) foreign libraries, information centers, and commercial organizations. Available services for each user category are given below. For information on electronic access for interlibrary loan requests, read Bullet 15.

DOCUMENT DELIVERY SERVICES TO INDIVIDUALS

The National Agricultural Library (NAL) supplies agricultural materials not found elsewhere to other libraries.

Filling requests for materials readily available from other sources diverts NAL's resources and diminishes its ability to serve as a national source for agricultural and agriculturally related materials. Therefore, NAL is viewed as a library of last resort. Submit requests first to local or state library sources prior to sending to NAL. In the United States, possible sources are public libraries, land-grant university or other large research libraries within a state. In other countries submit requests through major university, national, or provincial institutions.

If the needed publications are not available from these sources, submit requests to NAL with a statement indicating their non-availability. Submit one request per page following the instructions for libraries below.

NAL'S DOCUMENT DELIVERY SERVICE INFORMATION FOR THE LIBRARY

The following information is provided to assist your librarian in obtaining the required materials.

LOAN SERVICE -- Materials in NAL's collection are loaned only to other U.S. libraries. Requests for loans are made through local public, academic, or special libraries.

The following materials are not available for loan: serials (except USDA serials); rare, reference, and reserve books; microforms; and proceedings of conferences or symposia. Photocopy or microform of non-circulating publications may be purchased as described below.

DOCUMENT DELIVERY SERVICE -- Photocopies of articles are available for a fee. Make requests through local public, academic, or special libraries. The library will submit a separate interlibrary loan form for each article or item requested. If the citation is from an NAL database (CAIN/AGRICOLA, "Bibliography of Agriculture," or the NAL Catalog) and the call number is given, put that call number in the proper block on the request form. Willingness to pay charges must be indicated on the form. Include compliance with copyright law or a statement that the article is for "research purposes only" on the interlibrary loan form or letter. Requests cannot be processed without these statements.

CHARGES:

Photocopy, hard copy of microfilm and microfiche - $5.00 for
the first 10 pages or fraction copied from a single article or publication. $3.00 for each additional 10 pages or fraction.
Duplication of NAL-owned microfilm - $10.00 per reel.
Duplication of NAL-owned microfiche - $ 5.00 for the first
fiche and $ .50 for each additional fiche per title.

BILLING -- Charges include postage and handling, and are subject to change. Invoices are issued quarterly by the National Technical Information Service (NTIS), 5285 Port Royal Road, Springfield, VA 22161. Establishing a deposit account with NTIS is encouraged. DO NOT SEND PREPAYMENT.

SEND REQUESTS TO:

          USDA, National Agricultural Library
          Document Delivery Services Branch, PhotoLab
          10301 Baltimore Blvd., NAL Bldg.
          Beltsville, Maryland  20705-2351

Contact the Head, Document Delivery Services Branch in writing or by calling (301) 504-5755 with questions or comments about this policy.

2) DOCUMENT DELIVERY SERVICES AVAILABLE TO LIBRARIES, OTHER

INFORMATION CENTERS AND COMMERCIAL ORGANIZATIONS.

The National Agricultural Library (NAL) accepts requests from libraries and other organizations in accordance with the national and international interlibrary loan code and guidelines. In its national role, NAL supplies copies of agricultural materials not found elsewhere. Filling requests for materials readily available from other sources diverts NAL's resources and diminishes its ability to serve as a national source for agricultural and agriculturally related materials. Therefore, NAL is viewed as a library of last resort.

Submit requests to state/region/network sources prior to sending to NAL. Within the United States, possible sources are public libraries, land-grant university libraries or other large research libraries within a state. In other countries submit requests to major university, national or provincial institutions. If the needed publications are not available from these sources, submit requests to NAL with a statement indicating their non-availability.

REQUESTS -- Submit on the American Library Association (ALA) or the International Federation of Library Associations and Institutions (IFLA) interlibrary loan form or via electronic mail or telefacsimile (see over for more details). Include the complete name of the person authorizing the request on each form; the standard bibliographic source which lists the title as owned by NAL; and the call number if the citation is from an NAL database (CAIN/AGRICOLA, "Bibliography of Agriculture," or the NAL catalog).

LOAN SERVICE -- Materials in the NAL collection are loaned only to U.S. libraries. The loan period is one month.

The following materials are not available for loan: serials (except for USDA serials); rare, reference, and reserve books; microforms; and proceedings of conferences or symposia. Photocopy or microform of the non-circulating publications is supplied automatically (as described below) when the requesting organization indicates that photocopy is acceptable on the loan form.

AUDIOVISUALS (AVs) -- Order at least 3-4 weeks before the intended show date. Give show date and alternate show date when requesting specific titles. Request specific format needed if more than one format is given in the citation.

DOCUMENT DELIVERY SERVICE -- Submit a separate completed interlibrary loan form for each article required. Indicate willingness to pay charges on the form and compliance with copyright law or include a statement that the article is for "research purposes only." Requests are not processed without these statements.

CHARGES:

Photocopy, hard copy of microfilm and microfiche - $5.00 for
the first 10 pages or fraction copied from a single article or publication. $3.00 for each additional 10 pages or fraction.
Duplication of NAL-owned microfilm - $10.00 per reel.
Duplication of NAL-owned microfiche - $5.00 for the first
fiche and $ .50 for each additional fiche per title.

BILLING - Charges include postage and handling, and are subject to change. Invoices are issued quarterly by the National Technical Information Service (NTIS), 5285 Port Royal Road, Springfield, VA 22161. Establishing a deposit account with NTIS is encouraged. DO NOT SEND PREPAYMENT.

Send Requests to:

     USDA, National Agricultural Library
     Document Delivery Services Branch, ILL, PhotoLab
     10301 Baltimore Blvd.,  NAL Bldg.
     Beltsville, Maryland  20705-2351

Contact the Head, Document Delivery Services Branch in writing or by calling (301) 504-5755 with questions or comments about this policy.

3) DOCUMENT DELIVERY SERVICES AVAILABLE TO FOREIGN LIBRARIES,

INFORMATION CENTERS AND COMMERCIAL ORGANIZATIONS.

The National Agricultural Library (NAL) accepts requests from libraries and other organizations in accordance with the national and international interlibrary loan code and guidelines.

In its national role, NAL supplies copies of agricultural materials not found elsewhere. Filling requests for materials readily available from other sources diverts NAL's resources and diminishes its ability to serve as a national source for agricultural and agriculturally related materials. Therefore, NAL is viewed as a library of last resort.

Submit requests to major university libraries, national or provincial institutions or network sources prior to sending requests to NAL. If the needed publications are not available from these sources, submit requests to NAL with a statement indicating their non-availability.

AGLINET -- Requesters in countries with an AGLINET library are encouraged to make full use of that library and its networking capabilities. As an AGLINET participant, NAL provides free document delivery service for materials published in the United States to other AGLINET participants.

REQUESTS -- Submit requests on the American Library Association (ALA) or the International Federation of Library Associations and Institutions (IFLA) interlibrary loan form or via electronic mail or telefacsimile (see over for more details). Include the complete name of the person authorizing the request on each form; the standard bibliographic source which lists the title as owned by NAL; and the call number if the citation is from an NAL database (CAIN/AGRICOLA, "Bibliography of Agriculture", or the NAL catalog).

DOCUMENT DELIVERY SERVICE -- Submit a separate completed interlibrary loan form for each article requested. Indicate willingness to pay charges on the form, and compliance with copyright law or include a statement that the article is for "research purposes only". Requests cannot be processed without these statements.

CHARGES:

Photocopy, hard copy of microfilm and microfiche - $5.00 for
the first 10 pages or fraction copied from a single article or publication. $3.00 for each additional 10 pages or fraction.
Duplication of NAL-owned microfilm - $10.00 per reel.
Duplication of NAL-owned microfiche - $5.00 for the first
fiche and $ .50 for each additional fiche per title.

BILLING - Charges include postage and handling, and are subject to change. Invoices are issued quarterly by the National Technical Information Service (NTIS), 5285 Port Royal Road, Springfield, VA 22161. Establishing deposit account with NTIS is encouraged. Annual billing is available to foreign institutions on request by contacting NAL at the address below. DO NOT SEND PREPAYMENT.

Send Requests to:

     USDA, National Agricultural Library
     Document Delivery Services Branch, ILL, PhotoLab
     10301 Baltimore Blvd., NAL Bldg.
     Beltsville, Maryland  20705-2351

Contact the Head, Document Delivery Services Branch at (301) 504-5755 with questions or comments about this policy.