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
It is now well established that the seed storage proteins of major crop species are encoded as families of closely related genes. Similarities and divergencies are being defined at the levels of protein structure, amino acid sequence, and nucleotide sequence, (see Brown, Ersland, and Hall, 1982, and Ersland et al., 1983 for reviews). Phaseolin, the major storage protein of the French bean (Phaseolus vulgaris L.) can be separated into a group of about ten closely related polypeptides by two-dimensional PAGE. Analysis of some 150 cultivars yielded only three different patterns, characterized as T (Tendergreen), S (Sanilac) and C (Contender) types (Brown et al., 1981a). The component polypeptides range in apparent molecular weight from 45 to 51 kd, and in isoelectric point from pH 5.6–5.8 (Fig. 1). The T, S and C patterns contained 5, 8 and 8 polypeptides respectively.
KeywordsStorage Protein Seed Storage Protein French Bean Derive Amino Acid Sequence Major Storage Protein
Unable to display preview. Download preview PDF.
- Broach, J. R., Li, Y. Y., Feldman, J., Abraham, J., Nasmyth, K., and Hicks, J. B., 1982, Localization and sequence analysis of yeast origins of DNA. replication, Cold Spring Harbor Symp. Quant. Biol: 47. In press.Google Scholar
- Brown, J. W. S., Ma, Y., Bliss, F. A., and Hall, T. C., 1981a, Genetic variation in the subunits of globulin-1 storage protein of French bean, Theor. Appl. Genet., 59:83.Google Scholar
- Brown, J. W. S., Ersland, D. R., and Hall, T. C., 1982, Molecular aspects of storage protein synthesis during seed development, in: “The Physiology and Biochemistry of Seed Development, dormancy and Germination”, A. A. Khan, ed., Elsevier Biomedical Press, Amsterdam. In press.Google Scholar
- Efstradiatis, A., Posakony, J. W., Maniatis, T., Lawn, R. M., O’Connell, C., Spritz, R. A., DeRiel, J. K., Forget, B. G., Weissman, S. M., Slightom, J. L., Blechl, A. E., Smithies, O., Baralle, F. E., Shoulders, C. C., and Proudfoot, N. J., 1980, The structure and evolution of the human ß-globin gene family, Cell, 21:653.CrossRefGoogle Scholar
- Ersland, D. R., Brown, J. W. S., Casey, R., and Hall, T. C., 1983, The storage proteins of Phaseolus vutgaris L., Vicia Faba L., and Pisum sativum L., in: “The Genetics and Biochemistry of Seed Proteins”, W. Gottschalk and H. P. Müller, eds., Martinus Nijhoff, The Hague. In press.Google Scholar
- Geraghty, D., Peifer, M. A., Rubenstein, I., and Messing, J., 1981, The primary structure of a plant storage protein: zein. Nucl. Acids Res. 9:5163.Google Scholar
- Hall, T. C., Sun, S. M., Buchbinder, B. V., 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”, C. J. Leaver, ed., Plenum Publishing Corp., New York. p. 259.CrossRefGoogle Scholar
- Kemp, J. D., Sutton, D. W., Fink, C., Barker, R. F., and Hall, T. C., 1982, Agrobacterium-mediated transfer of foreign genes into plants, Beltsville Symposium VII, “Genetic Engineering: Applications to Agriculture”.Google Scholar
- Sun, S. M., 1974, Ph.D. Thesis, University of Wisconsin.Google Scholar