Abstract
The composition of storage proteins, a major food reservoir for the developing seeds, determines the nutritional value of plants and grains that are used as foods for man and domestic animals. The amount of protein varies with genotype or cultivar, but in general, cereals contain 10% of the dry weight of the seed as protein, while in legumes, the protein content varies between 20% and 30% of the dry weight. In many seeds, storage proteins account for 50% or more of the total protein, and thus determine the protein quality of seeds. Each year the total world cereal harvest amounts to some 1700 million tons of grain (Keris et al. 1985). This harvest yields about 85 million tons of cereal storage proteins harvested each year and contributes about 55% of the total protein intake of humans.
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References
Agros, P., K. Pederson, D. Marks, and B. A. Larkins. 1982. A structural model for maize zein proteins. J. Biol. Chem. 257:9984–9990.
Agros, P., S. V. L. Naravana, and N. C. Nielsen. 1985. Structural similarity between legumin and vicillin storage proteins from legumes. EMBO J. 4:1111–1117.
Altenbach, S. B., K. W. Pederson, G. Meeker, L. C. Staraci, and S. S. M. Sun. 1989. Enhancement of the methionine content of seed proteins by the expression of a chimeric gene encoding a methionine-rich protein in transgenic plants. PlantMol. Biol. 13:513–522.
Badley, R. A., D. Atkinson, H. Häuser, D. Oldani, J. P. Green, and J. M. Stubbs. 1975. The structure, physical and chemical properties of the soybean protein glycinin. Biochim. Biophys. Acta 412:214–228.
Bartels, D., and R. D. Tompson. 1983. The characterization of cDNA clones coding for wheat storage proteins. Nucleic Acid Res. 11:2961–2977.
Beachy, R. N., Z. L. Chen, R. B. Horsch, S. G. Rogers, N. J. Hoffman, and R. T. Fraley. 1985. Accumulation and assembly of soybean ß-conglycinin in seeds of transformed petunia plants. EMBO J. 4:3047–3053.
Bierzynski, A., P. S. Kim, and R. L. Baldwin. 1982. A salt bridge stabilizes the helix formed by isolated c-peptide of RNAse A. Proc. Natl. Acad. Sci. (USA) 79:2470–2474.
Blundell, T. L., S. J. Thornton, S. K. Burley, and G. A. Petsco. 1986. Atomic interactions. Science 234:1005–1009.
Bollini, R., and M. J. Chrispeels. 1978. Characterization and subcellular localization of vicillin and phyto-hemaglutinin, the two major reserve proteins of Phaseolus vulgaris. Planta 142:291–298.
Chen, Z. L., N. S. Pan, and R. N. Beachy. 1988. A DNA sequence element that confers seed-specific enhancement of a constitutive promoter. EMBO J. 7:297–302.
Chen, Z. L., M. A. Schüler, and R. N. Beachy. 1986. Functional analysis of regulatory elements in a plant embryo-specific gene. Proc. Natl. Acad. Sci. (USA) 83:8560–8564.
Chou, P. Y., and G. D. Fasman. 1978. Prediction of the secondary structure of proteins from amino acid sequence. Adv. Enzymol. 47:45–148.
Colot, V., L. S. Robert, T. A. Kavanagh, M. W. Beavan, and R. D. Tompson. 1987. Localization of sequences in wheat endosperm protein genes which confer tissue-specific expression in tobacco. EMBO J. 6:3559–3564.
Creighton, T. E. 1984. Proteins. New York: Freeman.
Crouch, M., K. Tenberge, N. E. Simone, and R. Ferl. 1983. Sequence of the 1.7K storage protein of Brassica napus. Mol. Appl. Genet. 2:273–283.
Degrado, W. F., and J. D. Lear. 1985. Induction of peptide conformation at apolar/water interfaces. J. Am. Chem. Soc. 107:7684–7689.
Degrado, W. F., Z. R. Wasserman, and J. D. Lear. 1989. Protein design, a minimalist approach. Science 241:622–628.
Esen, E. 1986. Separation of alcohol-soluble proteins (zeins) from maize into three fractions by differential solubility. Plant Physiol. 80:623–627.
Fasman, G. 1989. Protein conformational prediction. Trends Biochem. Sci. 14:295–299.
Finley, D., and A. Varshavsky. 1985. The ubiquitin system: Functions and mechanisms. Trends Biochem. Sci. 10:343–346.
Forde, B. G., M. Kreis, M. S. Williamson, R. P. Fry, and J. Pywell. 1985. Short tandem repeats shared by B- and C-hordein cDNAs suggest a common evolutionary origin for two groups of cereal storage protein genes. EMBO J. 4:9–15.
Goldberg, A. L., and A. C. St. John. 1976. Intracellular protein degradation in mammalian and bacterial cells: part 2. Ann. Rev. Biochem. 45:747–803.
Greenwood, J. S., and M. J. Chrispeels. 1985. Correct targeting of the bean storage protein phaseolin in the seeds of transformed tobacco. Plant Physiol. 79:65–71.
Gross, D. S., and W. T. Garrard. 1987. Poising chromatin for transcription. Trends Biochem. 12:293–296.
Ho S. P., and W. F. Degrado. 1987. Design of a 4-helix bundle protein: Synthesis of peptides which self-associate into helical protein. J. Am. Chem. Soc. 109:6751–6758.
Hoffmann, L. E., D. D. Donaldson, and E. M. Herman. 1988. A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants. Plant Mol. Biol. 11:717–729.
Hoffmann, L. E., D. D. Donaldson, R. Bookland, K. Rashka, and E. M. Herman. 1987. Synthesis and protein body deposition of maize 15-kd zein in transgenic tobacco seeds. EMBO J. 6:3213–3221.
Hol, W. G., and H. C. Sanders. 1981. Dipole of the α-helix and β-sheet: Their role in protein folding. Nature 294:532–536.
Jaynes, J. M., P. Nagpala, L. Destefano, T. Denny, C. Clark, and J.-H. Kim. 1992. Expression of a de novo designed peptide in transgenic tobacco plants confers enhanced resistance to Pseudomonas solanacearum infection. Submitted to Proc. Natl. Acad. Sci. (USA)
Jaynes, J. M., M. S. Yang, N. O. Espinoza, and J. H. Dodds. 1986. Plant protein improvement by genetic engineering: Use of synthetic genes. Trends Biotechnol. 4:314–320.
Jones, J. D. G., and D. E. Gilbert. 1987. T-DNA structure and gene expression in petunia plants transformed by Agrobacterium tumefaciens C58 derivatives. Mol.Gen. Genet. 207:478–485.
Kabsch, W., and C. Sander. 1983. How good are predictions of protein structure? FEBS Lett. 155:179–182.
Kane, J. F., and D. L. Hartley. 1988. Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotechnol. 6:95–101.
Kasarda, D. D., T. W. Okita, J. E. Bernardin, P. A. Baecker, and C. C. Nimmo. 1984. DNA and amino acid sequences of alpha and gamma gliadins. Proc. Natl. Acad. Sci. (USA) 81:4712–4716.
Keris, M., P. R. Shewry, B. G. Forde, G. Forde, and J. Miflin. 1985. Structure and evolution of seed storage proteins and their genes with particular reference to those of wheat, barley and rye. Oxford Survey Plant Mol. Cell Biol. 2:253–317.
Komoriya, A., and J. M. Chaiken. 1982. Sequence modeling using semisynthetic ribonuclease S. J. Biol. Chem. 257:2599–2604.
Larkins, B. A. 1983. Genetic engineering of seed storage protein. In Genetic Engineering of Plants, ed. B. A. Larkins, pp. 93–120. New York: Plenum.
Larkins, B. A., K. Pederson, M. D. Mark, and D. R. Wilson. 1984. The zein protein of maize endosperm. Trends Biochem. Sci. 9:306–308.
Lawrence, M. C., E. Suzuki, J. N. Varghes, P. C. Davis, A. Van Donkelaar, P. A. Tulloch, and P. M. Collman. 1990. The three-dimensional structure of the seed storage protein phaseolin at 3 À resolution. EMBO J. 9:9–15.
Lear, J. D., Z. R. Wasserman, and W. F. Degrado. 1988. Synthetic amphiphilic peptide model for protein ion channels. Science 240:1177–1181.
Lending, C. R., A. Kriz, B. A. Larkins, and C. E. Bracker. 1988. Structure of maize protein bodies and immunocytochemical localization of zeins. Protoplasma 143:51–62.
Lycett, G. W., R. D. Cory, A. H. Shirsat, D. M. Richards, and D. Boulter. 1985. The 5′-flanking regions of three pea legumin genes: Comparison of DNA sequences. Nucleic Acids Res. 13:6733–6743.
Marqusee, S., and R. Baldwin. 1987. Helix stabilization by GLU-LYS salt bridges in short peptides of de novo design. Proc. Natl. Acad. Sci. (USA) 84:8898–8902.
Marries, C., P. Gallois, J. Copley, and M. Keris. 1988. The 5′-flanking region of a barley B hordein gene controls tissue and developmental specific CAT expression in tobacco plants. Plant Mol. Biol. 10:359–366.
Mutter, M. 1988. Nature’s rules and chemist’s tools: A way for creating novel proteins. Trends Biochem. Sci. 13:260–264.
Neurath, H. 1989. Proteolytic processing and physiological regulation. Trends Biochem. Sci. 14:268–271.
Okamuro, J. K., K. D. Jofuku, and R. B. Goldberg. 1986. Soybean seed lectin gene and flanking nonseed protein genes are developmentally regulated in transformed tobacco plants. Proc. Natl. Acad. Sci. (USA) 83:8240–8244.
Pace, C. N., and A. J. Barret. 1984. Kinetics of tryptic hydrolysis of the arginine-valine bond in folded and unfolded ribonuclease T1. Biochem. J. 219:411–417.
Pakula, A. A. and R. T. Sauer. 1986. Bacteriophage 1 Cro mutation: Effect on activity and intracellular degradation. Proc. Natl. Acad. Sci. (USA) 82:8829–8833.
Pakula, A. A., and R. T. Sauer. 1989. Amino acid substitutions that increase the thermal stability of the I Cro protein. Proteins 5:202–210.
Parasell, D. A., and R. T. Sauer. 1989. The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli. J. Biol.Chem. 264:7590–7595.
Pederson, K., P. Agros, S. V. L. Naravana, and B. A. Larkins. 1986. Sequence analysis and characterization of a maize gene encoding a high-sulfur zein protein of Mw 15,000. J. Biol. Chem. 201:6279–6284.
Pernollet, J. C., and J. Mosse. 1983. Structure and location of legume and cereal seed storage protein. Seed Proteins (Phytochem. Soc. Europe Symp. Series) 20:155–187.
Presnell, S. R., and F. E. Cohen. 1989. Topological distribution of a four-α-helix bundle. Proc. Natl. Acad. Sci. (USA) 86:6592–6596.
Presta, L. G., and G. D. Rose. 1988. Helix signals in proteins. Science 240:1632–1641.
Rafalski, J. A., K. Scheets, M. Metzler, and D. M. Peterson. 1984. Developmentally regulated plant genes: The nucleotide sequence of a wheat gliadin geonomic clone. EMBO J. 3:1409–1415.
Richardson, J. S., and D. C. Richardson. 1988. Amino acid preferences for specific locations at the ends of a-helices. Science 240:1648–1652.
Richardson, J. S., and D. C. Richardson. 1989. The de novo design of protein structures. Trends Biochem. Sci. 14:304–309.
Sanders, P. R., J. A. Winter, A. R. Barnason, and S. G. Rogers. 1987. Comparison of cauliflower mosaic virus 35S and nopaline synthetase promoters in transgenic plants. Nucleic Acids Res. 15:1543–1558.
Scheraga, H. 1978. Use of random copolymers to determine helix-coil stability constants of the naturally occurring amino acids. Pure Appl. Chem. 50:315–324.
Scheraga, H.A. 1985. Effect of side chain-backbone electrostatic interaction on the stability of α-helices. Proc. Natl. Acad. Sci. (USA) 82:5585–5587.
Scott, R. J., and J. Draper. 1987. Transformation of carrot tissue derived from proembryogenic suspension cells: A useful model system for gene expression studies in plants. Plant Mol. Biol. 8:265–274.
Sengupta, G. C., N. A. Reichert, R. F. Baker, T. C. Hall, and J. D. Kemp. 1985. Developmentally regulated expression of the bean ß-phaseolin gene in tobacco seed. Proc. Natl. Acad. Sci. (USA) 82:3320–3324.
Shen, S.-H. 1984. Multiple joined genes prevent product degradation in E. coli.Proc. Natl. Acad. Sci. (USA) 81:4627–4631.
Shoemaker, K. R., P. S. Kim, E. J. York, J. M. Stewart, and R. L. Baldwin. 1987. Test of helix dipole model for stabilization of α-helices. Nature 326:563–566.
Staswick, P. E. 1989. Preferential loss of an abundant storage protein from soybean pods during seed development. Plant Physiol. 90:1251–1255.
Stockhaus, J., P. Eckes, A. Blau, J. Schell, and L. Willmitzer. 1987. Organ-specific and dosage-dependent expression of a leaf/stem specific gene from potato after tagging and transfer into potato and tobacco plants. Nucleic Acids Res. 15:3479–3491.
Sueki, M., S. Lee, S. P. Power, J. B. Denton, Y. Konishi, and H. Scheraga. 1984. Helix-coil stability constants for the naturally occurring amino acids in water. Macromolecules 17:148–155.
Twell, D., and G. Ooms. 1987. The 5′-flanking DNA of a patatin gene directs tuber specific expression of a chimeric gene in potato. Plant Mol. Biol. 9:365–375.
Wallace, J. C., G. Galili, E. E. Kawata, R. E. Cuellar, M. A. Shotwell, and B. A. Larkins. 1988. Aggregation of lysine containing zeins into protein bodies in Xenopus oocytes. Science 240:662–664.
Weiler, E. W., and J. Schroder. 1987. Hormone genes and crown gall disease. Trends Biochem. Sci. 12:271–275.
Wenzler, H. C., G. A. Mignery, L. M. Fisher, and W. D. Park. 1989. Analysis of a chimeric class I potatin-GUS gene in transgenic potato plants: High level expression of tubers and sucrose-inducible expression in cultured leaf and stem expiants. Plant Mol. Biol. 12:41–50.
Yang, M. S., N. O. Espinoza, J. H. Dodds, and J. M. Jaynes. 1989. Expression of a synthetic gene for improved protein quality in transformed potato plants. Plant Sci. 64:99–111.
Zimm, B. H., and J. R. Bragg. 1959. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:526–535.
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Kim, J., Cetiner, S., Jaynes, J.M. (1992). Enhancing the Nutritional Quality of Crop Plants: Design, Construction, and Expression of an Artificial Plant Storage Protein Gene. In: Bhatnagar, D., Cleveland, T.E. (eds) Molecular Approaches to Improving Food Quality and Safety. Springer, New York, NY. https://doi.org/10.1007/978-1-4684-8070-2_1
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DOI: https://doi.org/10.1007/978-1-4684-8070-2_1
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