Analysis of avenin proteins and the expression of their mRNAs in developing oat seeds.

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Abstract
We have isolated and characterized cDNA clones encoding avenins, the prolamine storage proteins of oat seeds. Sequence analysis shows that avenins are a related group of polypeptides and that their mRNAs differ from each other by point mutations and small insertions and deletions. Avenin proteins have structural homology to the .alpha./.beta.-gliadins and .gamma.-gliadins of wheat, the B-hordeins of barley, and the .gamma.-secalins of rye. Hybridization analysis of DNA from various diploid, tetraploid, and hexaploid oat species shows that the oat genome contains more globulin storage protein genes than avenin genes and that some restriction fragments containing these genes are conserved between species with common genomes. We estimate that there are 25 avenin genes and 50 globulin genes per haploid genome in Avena sativa and similar ratios of globulin to avenin genes in other Avena species. Avenin and globuline polypeptides begin to accumulate between 4 days and 6 days after anthesis. Messenger RNAs encoding avenin and globulin proteins become abundant 4 days after anthesis and reach peak concentrations at 8 days after anthesis. Avenin mRNAs are present in somewhat greater molar amounts than globulin mRNAs beginning at 4 days after anthesis. Because there is considerably more globulin than avenin in the mature oat seed, the expression of globulin and avenin genes may be regulated both transcriptionally and post-transcriptionally.