Summary
Endosperm protein mutants in rice may be recovered by biochemical selections with inhibitory levels of lysine and threonine. Among the phenotypes recovered from in vitro selections are lines with increased protein and percent lysine in the protein. This work was designed to identify changes in proteins of rice mutants and to further our understanding of the mechanisms of lysine plus threonine selections in rice. Among the most obvious amino acid changes in mutants was a higher lysine level in all protein solubility fractions and a decrease in tyrosine. Methionine and glutamate are reduced in some protein fractions. However, methionine is significantly higher in the mutant than the control in the glutelin fraction. Several other aspartate pathway amino acids are higher in the mutant than the unselected controls. Separation of proteins in SDS-PAGE gels showed shifts in the protein profiles in the mutants, including a decrease in the major 30 kDa low lysine globulin component, and an increase in several high-molecular-weight components, approximately 60–100 kDa. Increases in the lysine content of proteins of different solubility classes and different proteins within classes are detailed.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Bryan PA, Cawley RD, Brunner CE, Bryan JK (1970) Isolation and characterization of lysine-sensitive aspartokinase from a multicellular plant. Biochem Biophys Res Comm 41:1211–1217
Cattoir-Reynaerts AE, Degryse E, Verbruggen I, Jacobs M (1983) Selection and characterization of carrot embryoid cultures resistant to inhibition by lysine plus threonine. Biochem Physiol Pfl 178:81–90
Furuhashi K, Yatazawa M (1970) Methionine-lysine-threonine interrelationship in the amino acid nutrition of rice callus tissue. Plant Cell Physiol 11:569–578
Gengenbach BG, Walter TJ, Green CE, Hibberd KA (1978) Feedback regulation of lysine, threonine, and methionine biosynthetic enzymes in corn. Crop Sci 18:471–476
Green CE, Philips RL (1974) Potential selection system for mutants with increased lysine, threonine, and methionine in cereal crops. Crop Sci 14:827–830
Hibberd KA, Green CA (1982) Inheritance and expression of lysine plus threonine resistance selected in maize tissue culture. Proc Natl Acad Sci USA 79:559–563
Juliano BO (1985) Polysaccharides, proteins, and lipids of rice. In: Juliano BO (ed) Rice. Chemistry and technology. American Association of Cereal Chemists, St. Paul MN, pp 98–142
Luthe DA (1983) Storage protein accumulation in developing rice (Oryza sativa L.) seeds. Plant Sci Lett 32:147–158
Matthews BF, Widholm JM (1978) Regulation of lysine and threonine synthesis in carrot cell suspension cultures and whole carrot roots. Planta 141:315–321
Mertz TE (1976) Case histories of existing models. In: Genetic improvement of proteins. Proceedings of workshop. National Academy of Sciences, Washington, D.C., pp 57–70
Mertz TE, Bates LS, Nelson OE (1964) Mutant gene that changes protein composition and increases lysine content of maize endosperm. Science 145:279–280
Sano KI, Shiio I (1970) Microbial production of L-lysine. III. Production of mutants resistant to S-(2-aminoethyl)-L-cysteine. J Gen Appl Microbiol 16:373–391
Schaeffer GW, Sharpe FT (1981) Lysine in seed protein from S-aminoethyl-L-cysteine resistant anther-derived tissue cultures of rice. In Vitro 17:345–352
Schaeffer GW, Sharpe FT (1987) Increased lysine and seed storage protein in rice plants recovered from calli selected with inhibitory levels of lysine plus threonine and S-(2-aminoethyl)cysteine. Plant Physiol 84:509–515
Schaeffer GW, Sharpe FT, Carnahan HL, Johnson CW (1986) Anther and tissue culture-induced grain chalkiness and associated variants in rice. Plant Cell Tiss Org Cult 6:149–157
Schaeffer GW, Sharpe FT, Dudley JT (1988) Segregation for endosperm lysine in F2, F3, and F4 progeny from a cross of in-vitro-selected and unselected cultivar of rice. Theor Appl Genet 77:176–183
Author information
Authors and Affiliations
Additional information
Communicated by H. F. Linskens
Rights and permissions
About this article
Cite this article
Schaeffer, G.W., Sharpe, F.T. Modification of amino acid composition of endosperm proteins from in-vitro-selected high lysine mutants in rice. Theoret. Appl. Genetics 80, 841–846 (1990). https://doi.org/10.1007/BF00224202
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00224202