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Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations.

Azevedo, Ricardo A. and Lea, Peter John and Damerval, Catherine and Landry, Jacques and Bellato, Cláudia M. and Meinhardt, Lyndel W. and Le Guilloux, Martine and Delhaye, Sonia and Varisi, Vanderlei A and Gaziola, Salete A. and Gratão, Priscila Lupino and Toro, Alejandro A. (2004) Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations. Journal of Agricultural and Food Chemistry, 52 (15). pp. 4865-4871. ISSN 0021-8561

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Abstract

Two high lysine maize endosperm mutations, opaque-5 (o5) and opaque-7 (o7), were biochemically characterized for endosperm protein synthesis and lysine metabolism in immature seeds. Albumins, globulins, and glutelins, which have a high content of lysine, were shown to be increased in the mutants, whereas zeins, which contain trace concentrations of lysine, were reduced in relation to the wild-type lines B77xB79+ and B37+. These alterations in the storage protein fraction distribution possibly explain the increased concentration of lysine in the two mutants. Using two-dimensional polyacrylamide gel electrophoresis of proteins of mature grains, variable amounts of zein polypeptides were detected and considerable differences were noted between the four lines studied. The analysis of the enzymes involved in lysine metabolism indicated that both mutants have reduced lysine catabolism when compared to their respective wild types, thus allowing more lysine to be available for storage protein synthesis.

Item Type: Article
Journal or Publication Title: Journal of Agricultural and Food Chemistry
Uncontrolled Keywords: Aspartate kinase ; lysine ; lysine 2-oxoglutarate reductase ; maize ; storage proteins
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 10662
Deposited By: Mr Richard Ingham
Deposited On: 22 Jul 2008 09:21
Refereed?: Yes
Published?: Published
Last Modified: 17 Sep 2013 10:56
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/10662

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