Summary
Subunits of wheat endosperm proteins have been fractionated by two-dimensional electrophoresis. To determine which subunits in the two-dimensional electrophoretic pattern belong to gliadin or glutenin the endosperm proteins have also been fractionated by a modified Osborne procedure and by gel filtration on Sephadex G-100 and Sepharose CL-4B prior to separation by two-dimensional electrophoresis.
The control of production of five major grain protein subunits is shown to be determined by chromosomes 6A, 6B and 6D by comparing two-dimensional electrophoretic protein subunit patterns of aneuploid lines of the variety ‘Chinese Spring’. From these and previous studies it is concluded that some α, β and γ gliadins (molecular weights by SDS-PAGE 30,000 to 40,000) are specified by genes on the short arms of homoeologous Group 6 chromosomes, the ω gliadins (molecular weights by SDS-PAGE 50,000 to 70,000) are specified by genes on the short arms of homoeologous Group 1 chromosomes and the glutenin subunits (molecular weights by SDS-PAGE > 85,000) are specified by genes on the long arms of homoeologous Group 1 chromosomes.
No major gliadins or glutenin subunits were absent when any of the chromosomes in homoeologous Groups 2, 3, 4, 5 or 7 were deleted. However two gliadins whose presumed structural genes are on chromosome 6D were absent in aneuploid stocks of ‘Chinese Spring’ carrying two additional doses of chromosome 2A. Two out of thirty-three intervarietal or interspecific chromosome substitution lines examined, involving homoeologous Group 2 chromosomes, lacked the same two gliadins. All the subunits in the other thirty-one chromosome substitution lines were indistinguishable from those in ‘Chinese Spring’. It is therefore concluded that the major variation affecting gliadin and glutenins in wheat is concentrated on the chromosomes of homoeologous Groups 1 and 6 but Group 2 chromosomes are candidates for further study.
An endosperm protein controlled by chromosome 4D in ‘Chinese Spring’ is shown to be a high molecular weight globulin.
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Literature
Beckwith, A.C.; Nielson, H.C.; Wall, J.S.; Huebner, F.R. (1966): Isolation and characterization of a high-molecular weight protein from wheat gliadin. Cereal Chem. 43, 14–29
Bernardin, J.E.; Kasarda, D.D. (1973): The microstructure of wheat protein fibrils. Cereal Chem. 50, 736–745
Bietz, J.A.; Huebner, F.R.; Sanderson, J.E.; Wall, J.S. (1977): Wheat gliadin homology revealed through N-terminal amino acid sequence. Cereal Chem. 54, 1070–1083
Bietz, J.A.; Shepherd, K.W.; Wall, J.S. (1975): Single kernel analysis of glutenin: Use in wheat genetics and breeding. Cereal Chem. 52, 513–532
Bietz, J.A.; Wall, J.S. (1972): Wheat gluten molecules: Molecular weights determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Cereal Chem. 49, 416–430
Bietz, J.A.; Wall, J.S. (1973): Isolation and characterization of gliadin-like subunits from glutenin. Cereal Chem. 50, 537–547
Booth, M.R.; Ewart, J.A.D. (1969): Studies on four components of wheat gliadins. Biochim. Biophys. Acta 181, 226–233
Brown, J.W.S.; Kemble, R.J.; Law, C.N.; Flavell, R.B. (1979): Control of endosperm proteins in Triticum aestivum (var. ‘Chinese Spring’) and Aegilops umbellulata by homoeologous group 1 chromosomes. Genetics 93, 189–200
Brown, J.W.S., Law, C.N., Worland, A.J., Flavell, R.B. (1981): Genetic variation in wheat endosperm proteins: an analysis by two dimensional electrophoresis using intervarietal chromosome substitution lines. Theor. Appl. Genet. 59, 361–371
Charbonnier, L. (1973): Etude des protéines alcolo-solubles de la farine de blé. Biochimie 55, 1217–1225
Charbonnier, L. (1974): Isolation and characterization of ω-gliadin fractions. Biochim. Biophys. Acta 359, 142–151
Chen, C.H.; Bushuk, W. (1970): Nature of proteins in Triticale and its parental species. I. Solubility characteristics and amino acid composition of endosperm proteins. Canad. J. Plant Sci. 50, 9–14
Hamauzu, Z.; Kamazuka, Y.; Kanazawa, H.; Yonezawa, D. (1975): Molecular weight determination of component polypeptides of glutenin after fractionation by gel filtration. Agr. Biol. Chem. 39, 1527–1531
Hamauzu, Z.; Toyomasu, T.; Tonezawa, D. (1974): Molecular weight determination of gliadin fractions in gel filtration by SDS-Polyacrylamide gel electrophoresis and sedimentation equilibrium. Agr. Biol. Chem. 38, 2445–2450
Huebner, F.R.; Wall, J.S. (1976): Fractionation and quantitative differences of glutenin from wheat varieties varying in baking quality. Cereal Chem. 53, 258–268
Jones, R.W.; Taylor, N.W.; Senti, F.R. (1959): Electrophoresis and fractionation of wheat gluten. Arch. Biochem. Biophys. 84, 363–376
Law, C.N.; Young, C.F.; Brown J.W.S.; Snape, J.W.; Worland, A.J. (1978): The study of grain protein control in wheat using whole chromosome substitution lines. In: Seed protein Improvement by Nuclear Techniques, pp. 483–502. Vienna: Intern. Atomic Energy Agency
Nielson, H.C.; Babcock, G.E.; Senti, F.R. (1962): Molecular weight studies on glutenin before and after disulphide-bond splitting. Arch. Biochem. Biophys. 96, 252–258
O'Farrell, P.H. (1975): High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007–4021
Osborne, T.B. (1907): Proteins of the Wheat Kernel. Washington D.C.: Carnegie Institute of Washington
Payne, P.I.; Corfield, K.G. (1979): Subunit of wheat glutenin proteins isolated by gel filtration in a dissociating medium. Planta 145, 83–88
Riley, R.; Chapman, V.; Johnson, R. (1968): Introduction of yellow rust resistance of Aegilops comosa into wheat by genetically induced homoeologous recombinations. Nature 217, 383–384
Sears, E.R. (1954): The aneuploids of common wheat. Res. Bull. Mo. Coll. Agr. Exp. Sta. 572, 58
Sexson, K.; Wu, Y.V.; Huebner, F.R.; Wall, J.S. (1978): Molecular weights of wheat γ 2, β 6, α 1, α 8 and α 9 gliadins. Biochim. Biophys. Acta. 532, 279–285
Shepherd, K.W. (1968): Chromosomal control of endosperm proteins in wheat and rye. In: 3rd Int. Wheat Genet. Symp. (eds.: Finlay, K.W.; Shepherd, K.W.), pp. 86–96. New York: Plenum Publ.
Shepherd, K.W. (1973): Homoeology of wheat and alien chromosomes controlling endosperm protein phenotypes. In: Proc. 4th Int. Wheat Genet. Symp. (eds.: Sears, E.R.; Sears, L.M.) pp. 745–760. Columbia Mo.: Agr. Exp. Sta. Univ. Mo.
Waines, J.G. (1973): Chromosomal location of genes controlling endosperm protein production in Triticum aestivum cv. ‘Chinese Spring’. In: Proc. 4th Int. Wheat Genet. Symp. (eds.: Sears, E.R.; Sears, L.M.S.), pp. 873–877. Columbia Mo.: Agr. Exp. Stn. Univ. Mo.
Woychik, J.H.; Boundy, J.A.; Dimler, R.J. (1961): Starch gel electrophoresis of wheat gluten proteins with concentrated urea. Arch. Biochem. Biophys. 94, 477–482
Woychik, J.H.; Huebner, F.R.; Dimler, R.J. (1964): Reduction and starch gel electrophoresis of wheat gliadin and glutenin. Arch. Biochem. Biophys. 105, 151–156
Wrigley, C.W.; Shepherd, K.W. (1973): Electrofocusing of grain proteins from wheat genotypes. Ann. N.Y. Acad. Sci. 209, 154–162
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Brown, J.W.S., Flavell, R.B. Fractionation of wheat gliadin and glutenin subunits by two-dimensional electrophoresis and the role of group 6 and group 2 chromosomes in gliadin synthesis. Theoret. Appl. Genetics 59, 349–359 (1981). https://doi.org/10.1007/BF00276448
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DOI: https://doi.org/10.1007/BF00276448