Reference "Analysis of seed storage protein genes of oats"

Reference ID

8544

Title

Analysis of seed storage protein genes of oats

Source

The Journal of biological chemistry, 1990, vol. 265, pp. 9652-9658

Authors (4)

Shotwell-M-A	Boyer-S-K
Chesnut-R-S	Larkins-B-A

Abstract

We have isolated genomic clones encoding the two major classes of seed storage
proteins in oats, the 12 S globulins and the avenins. The globulin genes encode
glutamine-rich, sulfur-poor storage proteins that are highly conserved in
sequence and structure. The globulin genes contain three short introns whose
positions in the coding sequence are the same as in storage globulin genes in
legumes and other dicots. The avenin genomic clone contains four tightly linked
genes that belong to both of the two avenin gene subfamilies. The avenin genes
encode glutamine-rich, lysine-poor proteins that vary in length due to
differences in the number of peptide repeats. Although globulin and avenin genes
are expressed coordinately during oat seed development, their promoter regions
do not contain any conserved sequence elements that might determine
developmental timing. Previous studies showed that there are roughly equal
amounts of globulin and avenin mRNAs in developing oat seed, despite there being
much more globulin than avenin in mature seed. Storage protein synthesis in oats
must therefore be controlled partially by post-transcriptional mechanisms.
Sequence analysis of globulin and avenin genes has provided several clues as to
why globulin mRNAs may be translated more efficiently than avenin mRNAs.