Differential effects of high-lysine mutations on the accumulation of individual members of a group of proteins encoded by a disperse multigene family in the endosperm of barley (Hordeum vulgare L.)

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Abstract
The CM proteins are a group of major salt-soluble endosperm proteins encoded by a disperse multigene family. The effects of high-lysine mutations on the net accumulation in barley endosperm of 3 members of this group (MCa, CMb, and CMe) were investigated. Genes CMa, CMb and CMe are located in chromosomes 1, 4, and 3, respectively. Protein CMe is identical with a previously described trypsin inhibitor. The 3 proteins were quantified in the different genetic stocks by high-performance liquid chromatography [HPLC]. The different high-lysine mutations have different effects on the expression patterns of the 3 genes: CMe is markedly decreased and CMa and CMb are increased in mutant Riso 1508, whereas all 3 proteins are decreased in Riso 527 and increased in Riso 7 with respect to the wild-type Bomi; CMa and CMb are increased and CMe is unaffected in mutant Riso 56 with respect to the wild-type. Carlsberg II; and protein CMe is markedly decreased in Hiproly barley as compared with its sister line C14362. The implications of these results in connection with the evolution of CM proteins and with the characterization of high-lysine mutations are discussed.