Unusual features of cereal seed protein structure and evolution
- 1 June 1989
- Vol. 10 (6) , 201-207
- https://doi.org/10.1002/bies.950100606
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.Keywords
This publication has 16 references indexed in Scilit:
- Sequence and expression of a gene encoding an albumin storage protein in sunflowerMolecular Genetics and Genomics, 1987
- The nucleotide and deduced amino acid sequences of an HMW glutenin subunit gene from chromosome 1B of bread wheat (Triticum aestivum L.) and comparison with those of genes from chromosomes 1A and 1DTheoretical and Applied Genetics, 1987
- Biochemistry of Fern Spore Germination: Globulin Storage Proteins in Matteuccia struthiopteris L.Plant Physiology, 1987
- A C-terminal signal prevents secretion of luminal ER proteinsPublished by Elsevier ,1987
- Molecular analysis of γ-gliadin gene families at the complex Gli-1 locus of bread wheat (T. aestivum L.)Theoretical and Applied Genetics, 1986
- Molecular evolution of the seed storage proteins of barley, rye and wheatJournal of Molecular Biology, 1985
- The structural and evolutionary relationships of the prolamin storage proteins of barley, rye and wheatPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1984
- Molecular drive: a cohesive mode of species evolutionNature, 1982
- Protein disulphide‐isomerase is located in the endoplasmic reticulum of developing wheat endospermFEBS Letters, 1982
- Why genes in pieces?Nature, 1978