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Unusual features of cereal seed protein structure and evolution
Author(s) -
Kreis Martin,
Shewry Peter R.
Publication year - 1989
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950100606
Subject(s) - prolamin , storage protein , biology , globulin , amino acid , homology (biology) , endosperm , protein superfamily , sunflower , biochemistry , genetics , trypsin , glutelin , gene , peptide sequence , sunflower seed , albumin , botany , enzyme , agronomy , immunology
Abstract The alcohol‐soluble (prolamin) storage proteins of barley, wheat and rye vary in their structures, but all have two features in common: the presence of distinct structural domains differing in amino acid compositions, and of repeats within one of these domains. Detailed comparisons of amino acid sequences show that all appear to have evolved from a single ancestral gene consisting of three short related regions (called A, B and C). Regions related to A, B and C are also present in the minor prolamins of maize and in three other groups of seed proteins: inhibitors of α‐amylase and /or trypsin from cereals. 2S storage globulins from several dicotyledonous species and a 2S albumin from sunflower. It is suggested that these proteins together constitute a protein superfamily with limited sequence homology.