Differential gene expression in the developing barley endosperm

Abstract

Barley prolamin storage proteins account for 50% of the seed proteins. They are encoded by small multigene families that are only expressed in the developing endosperm. Previous work has shown that the major prolamins in barley are characterized by the presence of two or more unrelated structural domains, one of which contains repeated sequences. The non-repetitive domain is homologous with sequences present in other seed proteins found in the seed of mono- and dicotyledonous plants. Comparison of the 5' flanking region of a B1 hordein storage protein gene of barley with those of other prolamin genes (zeins and α-gliadins) reveals short sequences within 600 base pairs (bp) of the translation initiation codon that are strongly conserved. A short sequence at —300 bp seems to be unique to the prolamin genes and is possibly involved in the control of gene expression in the developing cereal endosperm. Six DNA-binding proteins have been identified that might recognize and interact with the putative regulatory sequences identified in the B1 hordein gene. Protease inhibitors account for a large proportion of the salt-soluble proteins of the barley seed, and contain up to 10% lysine. Cloned cDNAs for chymotrypsin inhibitors 1 and 2 have been isolated and characterized. All contain ochre stop condons in the sequences encoding a putative signal peptide. The two inhibitors are encoded by small multigene families that specify several subfamilies of mRNAs. The accumulation of chymotrypsin inhibitors in normal and mutant endosperms of barley is related to the abundances of their mRNAs.