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.
|Authors||Kreis, M., Forde, B. G., Rahman, S., Miflin, B. J. and Shewry, P. R.|
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 Publication||1985|
|Journal||Journal of Molecular Biology|
|Journal citation||183 (3), pp. 499-502|
|Digital Object Identifier (DOI)||doi:10.1016/0022-2836(85)90017-8|
|Open access||Published as non-open access|
|Funder project or code||Research Contract 471 of the Biomolecular Engineering Programme|
|05 Jun 1985|
|Copyright license||Publisher copyright|
|Academic Press Ltd- Elsevier Science Ltd|
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