Molecular evolution of the seed storage proteins of barley, rye and wheat

A - Papers appearing in refereed journals

Kreis, M., Forde, B. G., Rahman, S., Miflin, B. J. and Shewry, P. R. 1985. Molecular evolution of the seed storage proteins of barley, rye and wheat. Journal of Molecular Biology. 183 (3), pp. 499-502.

AuthorsKreis, M., Forde, B. G., Rahman, S., Miflin, B. J. and Shewry, P. R.
Abstract

The major storage proteins (prolamins) of barley, rye and wheat are characterized by the presence of two or more unrelated structural domains, one of which contains repeated sequences. Because of this repetitive structure and their restricted distribution (only in grasses), it has been suggested that the prolamins are of recent origin. Contrary to this hypothesis, we show that parts of the non-repetitive domain of one group of prolamins are homologous with sequences present in a large group of seed proteins from monocotyledonous and dicotyledonous plants; including Bowman-Birk protease inhibitors, cereal inhibitors of alpha-amylase and trypsin, and 2 S globulin storage proteins of castor bean and oil seed rape. This implies an ancient origin for these non-repetitive domains. The origins of the repetitive domains are not known but may lie within the grasses. 

Year of Publication1985
JournalJournal of Molecular Biology
Journal citation183 (3), pp. 499-502
Digital Object Identifier (DOI)doi:10.1016/0022-2836(85)90017-8
PubMed ID4020867
Open accessPublished as non-open access
FunderEuropean Union
Funder project or codeResearch Contract 471 of the Biomolecular Engineering Programme
Output statusPublished
Publication dates
Print05 Jun 1985
Copyright licensePublisher copyright
PublisherElsevier
Academic Press Ltd- Elsevier Science Ltd
ISSN0022-2836

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