Abstract
Cellulose acetate electrophoresis has been used to resolve the storage proteins of peas into their constituent groups. Comparisons of 171 randomly chosen genotypes representing primitive forms, subspecies, and cultivars of peas, of seven near-isogenic lines for round and wrinkled and of two F2 populations have shown that wrinkled seed has a lower proportion of legumin than round seed. The extent of the reduction varies with the background genotype; some of the wrinkled forms had less than one-third as much legumin as their isogenic round forms. This effect of the ra locus on storage protein composition provides the first example in peas of a mutant analogous to the op 2 and fl 2 mutants in maize. Sodium dodecyl sulphate polyacrylamide gel electrophoresis was used to discriminate the 40 kdalton (α subunits) of legumin. On the basis of the data obtained from F2 populations derived from genotypes with distinct α subunit patterns, it was shown that the structural genes for the α subunit polypeptides of legumin are on chromosome 7, and closely linked to the ra locus.
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Blagrove, R. J., and Gillespie, J. M. (1975). Isolation purification and characterization of the seed globulins of Lupinus angustifolius. Aust. J. Plant Physiol. 213.
Casey, R. (1979a). Genetic variability in the subunit structure of legumin from Pisum—a two-dimensional gel electrophoresis study. Heredity 43265.
Casey, R. (1979b). Immunoaffinity chromatography as a means of purifying legumin from Pisum (pea) seeds. Biochem. J. 177509.
Davies, D. R. (1976). Variation in the storage proteins of peas in relation to sulphur amino-acid content. Euphytica 25717.
Derbyshire, E., Wright, D. J., and Boulter, D. (1976). Legumin and vicilin, storage proteins of legume seeds. Phytochemistry 153.
Kooistra, E. (1962). On the differences between smooth and three types of wrinkled peas. Euphytica 11357.
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227680.
Lamprecht, H. (1948). The variation of linkage and the course of crossing over. Agric. Hort. Genet. 610.
McWhirter, K. S. (1971). A floury endosperm, high-lysine locus on chromosome 10. Maize Genet. Coop. News Letter 45184.
Mertz, E. T., Bates, L. S., and Nelson, O. E. (1964). Mutant gene that changes protein composition and increases lysine content of maize endosperm. Science 145279.
Miflin, B. J., and Shewry, P. F. (1979). The synthesis of proteins in normal and high lysine barley seeds. In Laidman, D. and Wyn Jones, R. G. (eds.), Recent Advances in the Biochemistry of Cereals. Academic, New York, p. 239.
Nelson, O. E., Mertz, E. T., and Bates, L. S. (1965). Second mutant gene affecting the amino acid pattern of maize endosperm proteins. Science 1501469.
Randall, P. J., Thomson, J. A., and Schroeder, H. E. (1979). Cotyledonary storage proteins in Pisum sativum. IV. Effects of sulfur, phosphorus, potassium and magnesium deficiencies. Aust. J. Plant Physiol. 611.
Shewry, P. R., Faulks, A. J., and Miflin, B. J. (1980). The effect of high-lysine mutations on the protein fractions of barley grain. Biochem. Genet. 18133.
Shia, G., and Slinkard, A. E. (1977). Relationship of seed shape and cotyledon colour to percent protein of peas. Crop Sci. 17183.
Singh, R., and Axtell, J. D. (1973). High lysine mutant gene (hl) that improves protein quality and biological value of grain sorghum. Crop Sci. 13535.
Soave, C., Righetti, P. G., Lorenzoni, C., Gentinetta, E., and Salamini, F. (1976). Expressivity of the opaque-2 gene at the level of zein molecular components. Maydica XXI61.
Soave, C., Suman, N., Viotti, A., and Salamini, F. (1978). Linkage relationships between regulatory and structural gene loci involved in zein synthesis in maize. Theor. Appl. Genet. 52263.
Soave, C., Viotti, A., Di Fonzo, N., and Salamini, F. (1979). Maize prolamin: synthesis and genetic regulation. In Seed Protein Improvement in Cereals and Grain Legumes. Vol. 1. Proc. Symp. Neuherberg, 1978, IAEA and FAO in cooperation with GSF, p. 165.
Stevens, W. L. (1940). Tables of the recombination fraction estimated from the product ratio. J. Genet. 39171.
Thomson, J. A., and Schroeder, H. E. (1978). Cotyledonary storage proteins in Pisum sativum. II. Hereditary variation in components of the legumin and vicilin fractions. Aust. J. Plant Physiol. 5281.
Thomson, J. A., Schroeder, H. E., and Dudman, W. F. (1978). Cotyledonary storage proteins in Pisum sativum. I. Molecular heterogeneity. Aust. J. Plant Physiol. 5263.
Tsai, C.-Y., and Dalby, A. (1974). Comparison of the effect of Shrunken-4, Opaque-2, Opaque-7, and Floury-2 genes on the zein content of maize during endosperm development. Cereal Chem. 51825.
Tsai, C. Y., Larkins, B. A., and Glover, D. V. (1978). Interaction of the Opaque-2 with starch-forming mutant genes on the synthesis of zein in maize endosperm. Biochem. Genet. 16883.
Yemm, E. W., and Cocking, E. C. (1955). The determination of amino acids with ninhydrin. Analyst 80209.
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Davies, D.R. The ra locus and legumin synthesis in Pisum sativum . Biochem Genet 18, 1207–1219 (1980). https://doi.org/10.1007/BF00484348
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DOI: https://doi.org/10.1007/BF00484348