Genetic control of lysine metabolism in maize endosperm mutants
| Autor: | Ricardo Antunes Azevedo, Alejandro A. Toro, Martine Le Guilloux, Lyndel W. Meinhardt, Jacques Landry, Sonia Delhaye, Cláudia de M. Bellato, Catherine Damerval, Salete Aparecida Gaziola, Vanderlei A. Varisi, Priscila Lupino Gratão, Peter J. Lea |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
chemistry.chemical_classification Homoserine dehydrogenase 0303 health sciences Globulin Mutant Lysine food and beverages Saccharopine dehydrogenase Plant Science Biology 01 natural sciences Molecular biology Endosperm Amino acid 03 medical and health sciences Biochemistry chemistry biology.protein Aspartate kinase Agronomy and Crop Science 030304 developmental biology 010606 plant biology & botany |
| Zdroj: | Functional plant biology : FPB. 31(4) |
| ISSN: | 1445-4416 |
| Popis: | The capacity of three maize endosperm opaque mutants (o10, o11 and o13) to accumulate soluble lysine in the seed in relation to their wildtype counterpart, W22+, was investigated. The W22o13 and W22o11 mutants exhibited 278% and 186% increases in soluble lysine, respectively, while for W22o10, a 36% decrease was observed, compared with the wildtype. A quantitative and qualitative study of the N constituents of the endosperm has been conducted and data obtained for the total protein, non-protein N, soluble amino acids, albumins / globulins, zeins and glutelins present in the seed of the mutants. Following 2D–PAGE, a total of 38 different forms of zein polypeptides were detected and considerable differences were noted between the three mutant lines. The metabolism of lysine was also studied by analysis of the enzymes aspartate kinase, homoserine dehydrogenase, lysine 2-oxoglutarate reductase and saccharopine dehydrogenase, which exhibited major changes in activity, depending on the genotype, suggesting that the mutant genes may have distinct regulatory activities. |
| Databáze: | OpenAIRE |
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