INVESTIGADORES
IGLESIAS Alberto Alvaro
artículos
Título:
Non-phosphorylating Glyceraldehyde-3-phosphate Dehydrogenase is Post-translationally Phosphorylated in Heterotrophic Cells of Wheat (Triticum aestivum)
Autor/es:
D.M. BUSTOS, A.A. IGLESIAS
Revista:
FEBS LETTERS
Editorial:
Elsevier Science B.V.
Referencias:
Año: 2002 vol. 530 p. 169 - 173
ISSN:
0014-5793
Resumen:
AbstractIn wheat, non-phosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPN) was found to be encoded by one gene giving rise to a single protein.However, Western blots revealed two di¡erent subunits of about 58 and 60 kDa in endosperm and shoots.The latter was attributed to in vivo phosphorylation of shoot GAPN.No modi¢cation occurred in leaves, where the enzyme is composed by a single 58 kDa polypeptide.GAPN partially puri¢ed from shoots and endosperm was dephosphorylated in vitro with alkaline phosphatase. Phosphorylated GAPN exhibited similar a⁄nity for substrates but a lower Vmax compared to the non-phosphorylated enzyme.Results suggest that reversible phosphorylation of GAPN could regulate NADPH production in the cytosol of heterotrophic plant cells.0 2002 Federation of European Biochemical Societies.Publishedby Elsevier Science B.V. All rights reserved.Key words: Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase; Post-translational modi¢cation;Enzyme phosphorylation; Triticum aestivum