Abstract
A vital foundation for civilization was the invention, apparently less than 20, 000 years ago, of crop cultivation. The realization that seeds could be collected and later sown to give new food plants permitted food to be grown and gathered at a given location for several years. This led to the replacement of nomadic foraging by the establishment of settlements, and the emergence of artisans. Seed proteins played a major role in these changes since, in addition to their degradation and assimilation by the germinating seedling, they represent major food resources that can be stored and used over winter for man and for livestock.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Anthony, J.L., Vonder Haar, R.A. and Hall, T.C. (1990) Nucleotide sequence of an alpha-phaseolin gene from Phaseolus vulgaris. Nucleic Acids Research, 18, 3396.
Bagga, S., Sutton, D., Kemp, J.D. and Sengupta-Gopalan, C. (1992) Constitutive expression of the beta-phaseolin gene in different tissues of transgenic alfalfa does not ensure phaseolin accumulation in non-seed tissue. Plant Molecular Biology, 19, 951–958.
Bassüner, R., Huth, A., Manteuffel, R. and Rapoport, T.A. (1983) Secretion of plant storage globulin polypeptides by Xenopus laevis oocytes. European Journal of Biochemistry, 133, 321–326.
Bäumlein, H., Nagy, I., Villarroel, R., Inzé, D. and Wobus, U. (1992) 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. The Plant Joumal, 2, 233–239.
Bäumlein, H., Braun, H., Kakhovskaya, I.A. and Shutov., A.D. (1995) Seed storage proteins of spermatophytes share a common ancestor with desiccation proteins of fungi. Journal of Molecular Evolution, 41, 1070–1075.
Bäumlein, H., Wobus, U., Pustell, J. and Kafatos, F.C. (1986) The legumin gene family: structure of a B type gene of Vicia faba and a possible legumin gene specific regulatory element. Nucleic Acids Research, 14, 2707–2720.
Bedinger, P.A., Hardeman, K.J. and Loukides, C.A. (1994) Travelling in style: the cell biology of pollen. Trends in Cell Biology, 4, 132–138.
Bednarek, S.Y. and Raikhel, N.V. (1992) Intracellular trafficking of secretory proteins. Plant Molecular Biology, 20, 133–150.
Blagrove, R.J., Lilley, G.G., Van Donkelaar, A., Sun, S.M. and Hall, T.C. (1984) Structural studies of a French bean storage protein: phaseolin. International journal Biol. Macromol., 6, 137–141.
Bobb, A.J., Eiben, H.G. and Bustos, M.M. (1995) PvAlf, an embryo-specific acidic transcriptional activator enhances gene expression from phaseolin and phytohemagglutinin promoters. The Plant Journal, 8, 331–343.
Bobb, A.J., Chern, M.S. and Bustos, M.M. (1997) Conserved RY-repeats mediate transactivation of seed-specific promoters by the developmental regulator PvALF. Nucleic Acids Research, 25, 641–647.
Bollini, R. and Chrispeels, M.J. (1979) The rough endoplasmic reticulum is the site of reserve protein synthesis in developing Phaseolus vulgaris cotyledons. Planta, 146, 487–501.
Bollini, R., Vitale, A. and Chrispeels., M.J. (1983) In vivo and in vitro processing of seed reserve protein in the endoplasmic reticulum: evidence for two glycosylation steps. Journal of Cell Biology, 96, 999–1007.
Bourdillon, J. (1951) A crystalline bean seed protein in combination with phytic acid. Journal of Biological Chemistry, 189, 65–72.
Boylan, M.T. and Sussex, I.M. (1987) Purification of an endopeptidase involved with storage-protein degradation in Phaseolus vulgaris L. cotyledons. Planta, 170, 342–352.
Braun, H., Czihal, A., Shutov, A.D. and Bäumlein, H. (1996) A vicilin-like seed protein of cycads: similarity to sucrose-binding proteins. Plant Molecular Biology, 31, 35–44.
Brown, J.W.S., Bliss, F.A. and Hall, T.C. (1980) Microheterogeneity of globulin-1 storage protein from French bean with isoelectricfocussing. Plant Physiology, 66, 838–840.
Brown, J.W.S., Bliss, F.A. and Hall, T.C. (1981) Linkage relationships between genes controlling seed proteins in French bean. Theoretical and Applied Genetics, 60, 251–259.
Buchbinder, B.U. (1980) Polysomal and messenger RNA directed in vitro synthesis and processing of phaseolin, the Gl seed storage protein of Phaseolus vulgaris L. Ph.D. Thesis, University of Wisconsin, Madison, pp. 1–41.
Burow, M.D., Sen, P., Chlan, C.A. and Murai, N. (1992) Developmental control of the ß-phaseolin gene requires positive, negative and temporal seed-specific transcriptional regulatory elements and a negative element for expression in stem and root. The Plant Journal, 2, 537–548.
Bustos, M.M., Verne, A.L., Griffing, L.R., Summers, M.D. and Hall, T.C. (1988) Expression, glycosylation and secretion of phaseolin in a baculovirus system. Plant Molecular Biology, 10, 475–488.
Bustos, M.M., Guiltinan, M.J., Jordano, J., Begum, D., Kalkan, F.A. and Hall, T.C. (1989) Regulation of beta-glucuronidase expression in transgenic tobacco plants by an A/T-rich, cis-acting sequence found upstream of a French bean beta-phaseolin gene. Plant Cell, 1, 839–853.
Bustos, M.M., Kalkan, F.A., VandenBosch, K.A. and Hall, T.C. (1991a) Differential accumulation of four phaseolin glycoforms in transgenic tobacco. Plant Molecular Biology, 16, 381–395.
Bustos, M.M., Begum, D., Kalkan, F.A., Battraw, M.J. and Hall, T.C. (1991b) Positive and negative cis-acting DNA domains are required for spatial and temporal regulation of gene expression by a seed storage protein promoter. EMBO Journal, 10, 1469–1479
Ceriotti, A., Pedrazzini, E., De Silvestris, M. and Vitale, A. (1995) Import into the endoplasmic reticulum. In Methods in Cell Biology, Vol. 50, Plant Cell Biology, (eds D.W. Galbraith, D.P. Bourque, and HJ. Bohnert), Academic Press, San Diego, pp. 295–308.
Chamberland, S., Daigle, N. and Bernier, F. (1992) The legumin boxes and the 3’ part of a soybean ß-conglycinin promoter are involved in seed gene expression in transgenic tobacco plants. Plant Molecular Biology 19, 937–949
Chern, M.S., Bobb, A.J. and Bustos, M.M. (1996a) The regulator of MAT2 (ROM2) protein binds to early maturation promoters and represses PvALF-activated transcription. Plant Cell, 8, 305–321.
Chern, M.S., Eiben, H.G. and Bustos, M.M. (1996b) The developmentally regulated bZIP factor ROM1 modulates transcription from lectin and storage protein genes in bean embryos. The Plant Journal, 10, 135–148.
Chrispeels, M.J. (1991) Sorting of proteins in the secretory system. Annual Review of Plant Physiology and Plant Molecular Biology, 42, 21–53.
Cramer, J.H., Lea K., Drong, R.F., Klassy, R.C., Slightom, J.L., Schaber M.D. and Kramer, R. (1986) Expression of the bean seed storage protein phaseolin in Saccharomyces cerevisiae. In Molecular Biology of Seed Storage Proteins and Lectins, (eds Shannon, L.M. and Chrispeels, M.J). The American Society of Plant Physiologists, pp. 183-191.
Cramer, J.H., Lea, K., Schaber, M.D. and Kramer, R.A. (1987) Signal peptide specificity in post translational processing of the plant protein phaseolin in Saccharomyces cerevisiae. Molecular and Cellular Biology, 1, 121–128.
Czako, M. and An, G. (1991) Expression of DNA coding for diphtheria toxin chain A is toxic to plant cells. Plant Physiology, 95, 687–692.
Danielsson, C.E. (1949) Seed globulins of the gramineae and leguminosae. Biochemical Journal, 44, 387–400.
Dickinson, C.D., Evans, R.P. and Nielsen, N.C. (1988) RY repeats are conserved in the 5’-flanking regions of legume seed-protein genes. Nucleic Acids Research, 16, 371.
Drapkin, R., Merino, A. and Reinberg, D. (1993) Regulation of RNA polymerase II transcription. Current Opinions in Cell Biology, 5, 469–476.
Dyer, J.M., Nelson, J.W. and Murai, N. (1995) Extensive modifications for methionine enhancement in the beta-barrels do not alter the structural stability of the bean seed storage protein phaseolin. Journal of Protein Chemistry, 14, 665–678.
Eyal, Y., Curie, C. and McCormick, S. (1995) Pollen specificity elements reside in 30 bp of the proximal promoters of two pollen-expressed genes. Plant Cell, 7, 373–384.
Felsenfeld, G. (1992) Chromatin as an essential part of the transcriptional mechanism. Nature 355, 219–224.
Frisch, D.A., van der Geest, A.H.M., Dias, K. and Hall, T.C. (1995) Chromosomal integration is required for spatial regulation of expression from the ß-phaseolin promoter. the Plant Journal, 7, 503–512.
Fujiwara, T. and Beachy, R.N. (1994) Tissue-specific and temporal regulation of the ß-conglycinin gene: roles of the RY repeat and other cis-acting elements. Plant Molecular Biology, 24, 261–272.
Gatehouse, J.A., Evans, I.M., Croy, R.R.D. and Boulter, D. (1986) Differential expression of genes during legume seed development. Philosophical Transactions of the Royal Society of London, B314, 367–384.
Hall, T.C. and Kemp, J.D. (1981) Enhancing protein seed quality and quantity, in Genetic Engineering, International conference organized by Battelle Memorial Institute, Proceedings, 5, 36–67.
Hall, T. C, Sun, S. M, Buchbinder, B. U. and Belozerskii, M. A. (1977) The translation of mRNA for storage globulin of the bean, Phaseolus vulgaris. In: Translation of Natural and Synthetic Polynucleotides. (ed A. Legocki), University, of Agriculture in Poznan, Poland, pp. 217–223.
Hall, T.C, Ma, Y., Buchbinder, B.U., Pyne, J.W., Sun, S.M. and Bliss, F.A. (1978) Messenger RNA for Gl protein of French bean seeds: cell-free translation and product characterization. Proceedings of the National Academy of Sciences, USA, 75, 3196–3200.
Hall, T.C, Sun, S.M, Ma, Y., McLeester, R.C, Pyne, J.W., Bliss, F.A. and Buchbinder, B.U. (1979) The major storage protein of French bean seeds: characterization in vivo and translation in vitro, in The Plant Seed: Development, Preservation and Germination, (eds, I. Rubenstein, R.L. Phillips, CE. Green and B.G. Gengenbach), Academic Press, Inc., New York. I, 3–26.
Hall, T.C, Sun, S.M., Ma, Y., Buchbinder, B.U. Pyne, J.W., Bliss, F.A. and Kemp, J.D. (1980) Bean seed globulin mRNA: Translation, characterization, and its use as a probe towards genetic engineering of crop plants, in Genome Organization and Expression in Plants, (ed C.J. Leaver), Plenum, New York, pp. 259–272.
Hall, T.C, Slightom, J.L., Ersland D.R., Murray M.G., Hoffman L.M., Adang, M.J., Brown J.W.S., Ma T., Matthews J.A., Cramer J.H., Barker R.F., Sutton D.W. and Kemp, J.D. (1983) Phaseolin: Nucleotide sequence explains molecular weight and charge heterogeneity of a small multigene family and also assists vector construction for gene expression in alien tissue, in Structure and Function of Plant Genomes, (eds O. Ciferri & L.S. Dure), Plenum, New York, pp. 123–142.
Hall, T.C, Reichert, N.A., Sengupta-Gopalan, C, Cramer, J. H., Lea, K., Barker, R.F., Slightom, J.L., Klassy, R. and Kemp, J.D. (1985) Regulation of bean ß-phaseolin gene expression in yeast and tobacco seed. In: Molecular Form and Function of the Plant Genome, (eds L. van Vloten-Doting, G. S. P. Groot and T. C. Hall), Plenum Press, New York, pp. 517–529.
Hall, T.C, Li, G. and Chandrasekharan, M.B. (1998) Participation of Chromatin in the Regulation of Phaseolin Gene Expression. Gatersleben meeting. Journal of Plant Physiology, in press.
Hammond, C, Braakman, I. and Helenius, A. (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proceedings of the National Academy of Sciences, USA, 91, 913–917.
Hiei, Y., Ohta, S., Komari, T. and Kumashiro, T. (1994) Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA. The Plant Journal, 6, 271–282.
Hoffman, L.M., Donaldson, D.D. and Herman, E.M. (1988) A modified storage protein is synthesised, processed and degraded in the seeds of transgenic plants. Plant Molecular Biology, 11 717–729.
Hohl, L, Robinson, D., Chrispeels, M. and Hinz, G. (1996) Transport of storage proteins to the vacuole is mediated by vesicles without a clathrin coat. Journal of Cell Science, 109, 2539–2550.
Hori, H. and Elbein A.D. (1983). Processing of N-linked oligosaccharides in soybean cultured cells. Archives of Biochemistry and Biophysics, 220, 415–425.
Jacoby, W.B. (1968) A technique for the crystallization of proteins. Analytical Biochemistry, 26, 295–298.
Jaenicke, R. (1993) Role of accessory proteins in protein folding. Current Opinions in Structural Biology, 3, 104–112.
Jefferson, R.A. (1987) Assaying chimeric genes in plants: the GUS gene fusion system. Plant Molecular Biology Reporter, 5, 387–405.
Johnson, S., Grayson, G., Robinson, L., Chahade R. and McPherson, A. (1982) Biochemical and crystallographic data for phaseolin, the seed storage protein from Phaseolus vulgaris. Biochemistry, 21, 4045–4059.
Joubert, F.J. (1955) Ultracentrifuge studies on seed protein of the family Leguminosae. Part I-Yellow lupine seed (Lupinus luteus) proteins. Journal of the South African Chemical Institute, 8, 68–74.
Kami, J.A. and Gepts, P. (1994) Phaseolin nucleotide sequence diversity in Phaseolus. I. Intraspecific diversity in Phaseolus vulgaris. Genome, 37, 751–757.
Kami, J., Velasquez, V.B., Debouck, D.G. and Gepts, P. (1995) Identification of presumed ancestral DNA sequences of phaseolin in Phaseolus vulgaris. Proceedings of the National Academy of Sciences, USA, 92, 1101–1104.
Kaplan, L. (1965) Archeology and domestication in American Phaseolus (beans). Economic Botany, 19, 358–368.
Kawagoe, Y. and Murai, N. (1992) Four distinct nuclear proteins recognize in vitro the proximal promoter of the bean seed storage protein ß-phaseolin gene conferring spatial and temporal control. The Plant Journal, 2, 927–936.
Kawagoe, Y., Campbell, B.R. and Murai, N. (1994) Synergism between CACGTG (G-box) and CACCTG cis-elements is required for activation of the bean seed storage protein ß-phaseolin gene. The Plant Journal, 5, 885–890.
Kim, J.W. and Minamikawa, T. (1996) Transformation and regeneration of French bean plants by the particle bombardment process. Plant Science, 117, 131–138.
Kumpatla, S.P., Chandrasekharan, M.B., Iyer, L.M., Li, G. and Hall, T. C. (1998) Genome intruder scanning and modulation systems and transgene silencing. Trends in Plant Science, 3, 97–104.
Lawrence, M.C., Suzuki, E., Varghese, J.N., Davis, P.C., Van Donkelaar, A., Tulloch, P.A. and Colman, P.M. (1990) The three-dimensional structure of the seed storage protein phaseolin at 3C resolution. EMBO Journal, 9, 9–15.
Lawrence, M.C., Izard, T., Beuchat, M., Blagrove, R.J. and Colman, P.M. (1994) Structure of phaseolin at 2.2C: Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. Journal of Molecular Biology, 238, 748–776.
Lelievre, J-M., Oliveira, L.O. and Nielsen, N.C. (1992) 5’-CATGCAT-3’ elements modulate the expression of glycinin genes. Plant Physiology, 98, 387–391.
Lerouge, P., Fitchette-Laine, A.C., ChekkafI, A., Avidgor, V. and Faye, L. (1996) N-linked oligosaccharide is not necessary for glycoprotein secretion in plants. The Plant Journal 10, 713–719.
Li, G., Chandler, S.P., Wolffe, A. and Hall, T.C. (1998). Architectural specificity in chromatin structure at the TATA boxes in vivo: Nucleosome displacement upon ß-phaseolin gene activation. Proceedings of the National Academy of Sciences, USA, 95, 4772–4777.
Liener, I.E. and Thompson, R.M. (1980) In vitro and in vivo studies on the digestibility of the major storage protein of the navy bean (Phaseolus vulgaris). Qualitas Plantarurn — Plant Foods for Human Nutrition, 30, 13–25.
Lioi, L. and Bollini, R. (1984) Contribution of processing events to the molecular heterogeneity of four banding types of phaseolin, the major storage protein of Phaseolus vulgaris L. Plant Molecular Biology, 3, 345–353.
Lupattelli, F., Pedrazzini, E., Bollini, R., Vitale, A. and Ceriotti, A. (1997) The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains. Plant Cell, 9, 597–609.
Matthews, J.A., Brown J.W.S. and Hall, T.C. (1981) Phaseolin mRNA is translated to yield glycosylated polypeptides in Xenopus oocytes. Nature, 294, 175–176.
McLeester, R.C., Hall, T.C, Sun, S.M. and Bliss, F.A. (1973) Comparison of globulin proteins from Phaseolus vulgaris with those from Vicia faba. Phytochemistry, 2, 85–93.
Merlot, S. and Giraudat, J. (1997) Genetic analysis of abscisic acid signal transduction. Plant Physiology, 114, 751–757.
Murai, N.M., Sutton D.W., Murray, M.G., Slightom J.L., Merlo D.J., Reichert N.A., Sengupta-Gopalan C., Stock C.A., Richard B.F., Kemp J.D. and Hall, T.C. (1983) Phaseolin from bean is expressed after transfer to sunflower via tumor-inducing plasmid vectors. Science, 222, 476–482.
Murray, M.G. and Kennard W.C (1984) Altered chromatin configuration of the higher plant gene phaseolin. Biochemistry, 23, 4225–4232.
Mutschier, M.A., Bliss, F.A. and Hall, T.C (1980) Variation in accumulation of seed storage protein among genotypes of Phaseolus vulgaris (L.) Plant Physiology, 65, 627–630.
Nielsen, S.S. and Liener, I.E. (1984) Degradation of the major seed storage protein of Phaseolus vulgaris during germination. Plant Physiology, 74, 494–498.
Nielsen, N.C (1998) Soybean globulins. This book, Chapter 13.
Nodari, R.O., Tsai, S.M., Guzman, P., Gilbertson, R.L. and Gepts, P. (1993) Toward an integrated linkage map of common bean. 2. Development of an RFLP-based linkage map. Theoretical and Applied Genetics, 85, 513–520.
Nordlee, J.A., Taylor, S.L., Townsend, J.A., Thomas, L.A. and Bush, R.K. (1996) Identification of a Brazil-nut allergen in transgenic soybeans. New England Journal of Medicine, 334, 688–692.
Okita, T.W. and Rogers, J.C (1996) Compartmentation of proteins in the endomembrane system of plant cells. Annual Review of Plant Physiology and Plant Molecular Biology, 47, 327–350.
Osborne, T.B. (1894) The proteins of kidney bean. Journal of American Chemical Society, 16, 633–764.
Osborne, T.B. and Campbell, G.F. (1898a) Proteids of the soy bean. Journal of the American Chemical Society, 20, 348–362.
Osborne, T.B. and Campbell, G.F. (1898b) Proteids of the horse bean (Vicia faba). Journal of the American Chemical Society 20, 393–405.
Osborne, T.B. (1924) The vegetable proteins, 2nd edition, Longman, Green & Co., pp. 21–28.
Paaren H.M., Slightom JL., Hall, T.C, Inglis A.S. and Blagrove R.J. (1987) Purification of a seed glycoprotein: N-terminal and deglycosylation analysis of phaseolin. Phytochemistry, 26, 335–343.
Parcy, F., Valon, C, Raynal, M., Gaubier-Comella, P., Delseny, M. and Giraudat, J. (1994) Regulation of gene expression programs during arabidopsis seed development: Roles of the ABI3 locus and of endogenous abscisic acid. Plant Cell, 6, 1567–1582.
Parodi, A.J., Mendelzon, D.H., Lederkremer, G.Z. and Martin-Barrientos, J. (1984) Evidence that transient glucosylation of protein-linked Man9GlcNAc2, MangGlcNAc2, and Man7GlcNAc2 occurs in rat liver and Phaseolus vulgaris cells. Journal of Biological Chemistry, 259, 6351–6357.
Pedrazzini, E., Giovinazzo G., Bollini R., Ceriotti A. and Vitale A. (1994) Binding of BiP to an assembly-defective protein plant cells. The Plant Journal, 5, 103–110.
Pedrazzini, E., Giovinazzo, G., Bielli, A., de Virgilio, M., Frigerio, L., Pesca, M., Faoro, F., Bollini, R., Ceriotti, A. and Vitale, A. (1997) Protein quality control along the route to the plant vacuole. Plant Cell, 9, 1869–1880.
Plietz, P., Damaschum, G., Zirwer, D., Gast, K. and Schlesier, B. (1983) Structure of 7S seed globulin from Phaseolus vulgaris L. in solution. International Journal of Biological Macromolecules 5, 356–360.
Pueyo, J.J., Chrispeels, M.J. and Herman, E.M. (1995) Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole. Planta, 196, 586–596.
Pusztai, A. and Watt, W.B. (1970) Glycoprotein H The isolation and characterization of a major antigenic and non-haemagglutinating glycoprotein from Phaseolus vulgaris. Biochimica et Biophysica Acta, 207, 413–431.
Quattrocchio, F., Tolk, M. A., Coraggio, L, Mol, J.N.M., Viotti, A. and Koes, R.E. (1990) The maize zein gene zE19 contains two distinct promoters which are independently activated in endosperm and anthers of transgenic Petunia plants. Plant Molecular Biology, 15, 81–93.
Ritthausen, H. (1863) Die Proteinsubstanz der ersben, wicken, Saubohnen, linsen und bohnen, das pflazen-casein oder legumin. Journal fur Praktical Chimie, 53, 193.
Ritthausen, H. (1884) Ueber die Zusammensetzung der mittelst Salzlösung dargestellten eiweisskörper der Saubohnen (Vicia Faba) und weissen Bohnen (Phaseolus). Journal für Praktical Chemie, 137, 449–457.
Rock, CD. and Quatrano, R.S. (1995) The role of hormones during seed development. In Plant hormones (ed P. J. Davies), Kluwer Academic, Dordrecht, The Netherlands, pp. 617–697.
Romero, J. and Ryan, D.S. (1978) Susceptibility of the major storage protein of the bean, Phaseolus vulgaris L., to in vitro enyzymic hydrolysis. Journal of Agricultural and Food Chemistry, 26, 784–788.
Russell, D.R., Wallace, K.M., Bathe, J.H., Martinell B.J. and McCabe, D.E. (1993) Stable transformation of Phaseolus vulgaris via electric-discharge mediated acceleration. Plant Cell Reports, 12, 165–169.
Schroeder, H.E., Schotz, A.H., Wardley-Richardson, T., Spencer, D. and Higgins, T.J.V. (1993) Transfonnation and regeneration of two cultivars of pea (Pisum sativum L.) Plant Physiology, 101, 751–757.
Sengupta C, DeLuca, V., Bailey, D.S. and Verma, D.P.S. (1981) Post-translational processing of 7S and 1 IS components of soybean storage proteins. Plant Molecular Biology, 1, 19–34.
Sengupta-Gopalan, C, Reichert, N.A., Barker, R.F., Hall, T.C. and Kemp, J.D. (1985) Developmentally regulated expression of bean beta-phaseolin in tobacco seed. Proceedings of the National Academy of Sciences, USA, 80, 1897–1901.
Sjögren, B. and Svedberg, T. (1930) The Molecular weight of legumin. Journal of the American Chemical Society, 52, 3279–3283.
Slightom, J.L., Drong R.F., Klassy R.C. and Hoffman, L.M. (1985) Nucleotide sequence from phaseolin cDNA clones: the major storage proteins from Phaseolus vulgaris are encoded by two unique gene families. Nucleic Acids Research, 13, 6483–6498.
Slightom, J.L., Sun S.M. and Hall T.C. (1983) Complete nucleotide sequence of a French bean storage protein gene: Phaseolin. Proceedings of the National Academy of Sciences, USA, 82, 3320–3324.
Sousa, M. and Parodi, A.J. (1995) The molecular basis for the recognition of misfolded glycoproteins by IJDP-glucoseiglycoprotein glucosyltransferase. EMBO Journal, 14, 4196–4203.
Stanley, D.J. and Warne, A.G. (1993) Sea level and initiation of predynastic culture in the Nile delta. Nature, 363, 435–438.
Stockman, D. R., Hall T. C. and Ryan, D. S. (1976) Affinity chromatography of the major seed protein of the bean (Phaseolus vulgaris L.). Plant Physiology, 58, 272–275.
Sturm, A., Johnson K.D., Szumilo, T., Elbein A.D. and Chrispeels, M.J. (1987a) Subcellular localization of glycosidases and glycosyltransferases involved in the processing of N-linked oligosaccharides. Plant Physiology, 85, 741–745.
Sturm, A., Van Kuik J.A., Vliegenthart, J.F. and Chrispeels, M.J. (1987b) Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin. Journal of Biological Chemistry, 262, 13392–13403.
Sun, S.M., Buchbinder B.U. and Hall, T.C. (1975) Cell-free synthesis of the major storage— protein of the bean, Phaseolus vulgaris L. Plant Physiology, 56, 780–785.
Sun, S.M. and Hall, T.C. (1975) Solubility characteristics of globulins from Phaseolus seeds in regard to their isolation and characterization. Journal of Agricultural and Food Chemistry, 23, 184–189.
Sun, S.M., McLeester R.C., Bliss F.A. and Hall, T.C. (1974) Reversible and irreversible dissociation of globulins from Phaseolus vulgaris seed. Journal of Biological Chemistry, 249, 2118–2121.
Sun, S.M., Mutschier M.A., Bliss F.A. and Hall, T.C. (1978) Protein synthesis and accumulation in bean cotyledons during growth. Plant Physiology, 61, 918–923.
Sun, S.M., Slightom, J.L. and Hall, T.C. (1981) Intervening sequence in a plant gene-comparison of the partial sequence of cDNA and genomic DNA of French bean phaseolin. Nature, 289, 37–41.
Sussex, I. and Dale, R.M.K. (1979) Hormonal control of storage protein synthesis in Phaseolus vulgaris, in The Plant Seed: Development, Preservation and Germination, (eds I. Rubenstein, R.L. Phillips, C.E. Green and B.G. Gengenbach), Academic Press, Inc., New York, pp 129–141.
Suzuki, M, Kao, C.Y. and McCarty, D.R. (1997) The conserved B3 domain of VIVIPAROUS 1 has a cooperative DNA binding activity. Plant Cell, 9, 799–807.
Suzuki, E., Van Donkelaar A., Varghese, J.N., Lilley, G.G., Blagrove, R.J. and Colman, P.M. (1983) Crystallization of phaseolin from Phaseolus vulgaris. Journal of Biological Chemistry, 258, 2634–2636.
Talbot, D.R., Adang, M.J., Slightom, J.L. and Hall, T.C. (1984) Size and organization of a multigene family encoding phaseolin, the major seed protein of Phaseolus vulgaris L. Molecular and General Genetics, 198, 42–49.
Thoma, F. (1992) Nucleosome positioning. Biochimica et Biophysica Acta, 113, 1–19.
Travers, A.A. (1992) The reprogramining of transcriptional competence. Cell, 69, 573–575.
van der Geest, A.H.M., Hall, G.E. Jr., Spiker, S. and Hall, T.C. (1994) The ß-phaseolin gene is flanked by matrix attachment regions. The Plant Journal, 6, 413–423.
van der Geest, A. H. M., Frisch, D. A., Kemp, J. D. and Hall, T. C. (1995) Cell ablation reveals that expression from phaseolin promoter is confined to embryogenesis and micrsporogenesis. Plant Physiology, 109, 1151–1158.
van der Geest, A.H.M. and Hall, T.C. (1996) A 68 bp element of the ß-phaseolin promoter functions as a seed-specific enhancer. Plant Molecular Biology, 32, 579–588.
van der Geest, A.H.M. and Hall, T.C. (1997) The beta-phaseolin 5’ matrix attachment region acts as an enhancer facilitator. Plant Molecular Biology, 33, 553–557.
van Holde, K. E. and Zlatanova, J. (1996) Chromatin architectural proteins and transcription factors: a structural connection. BioEssays, 18, 697–700.
Vitale, A., Bielli, A. and Cenotti, A. (1995) The binding protein associates with monomeric phaseolin. Plant Physiology, 107, 1411–1418.
Vitale, A., Ceriotti A. and Denecke, J. (1993) The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport. Journal of Experimental Botany. 44, 1471–1484.
Vitale, A. and Chrispeels, M.J. (1984) Transient N-acetylglucosamine in the biosynthesis of phytohaeinagglutinin: attachment in the Golgi apparatus and removal in protein bodies. Journal of Cell Biology, 99, 133–140.
Vitale, A. and Chrispeels, M.J. (1992) Sorting of proteins to the vacuoles of plant cells. BioEssays, 14, 151–159.
Wade, P.A., Pruss, D. and Wolffe, A.P. (1997) Histone acetylation: chromatin in action. Trends in Biochemical Sciences, 22, 128–132.
Wolffe, A.P. (1994) Transcription: in tune with the histones. Cell, 77, 13–16.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1999 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Hall, T.C., Chandrasekharan, M.B., Li, G. (1999). Phaseolin: its Past, Properties, Regulation and Future. In: Shewry, P.R., Casey, R. (eds) Seed Proteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4431-5_10
Download citation
DOI: https://doi.org/10.1007/978-94-011-4431-5_10
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-5904-6
Online ISBN: 978-94-011-4431-5
eBook Packages: Springer Book Archive