INVESTIGADORES
BUSTOS Diego Martin
artículos
Título:
Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum)
Autor/es:
DIEGO M. BUSTOS; IGLESIAS, AA
Revista:
FEBS LETTERS
Editorial:
Elsevier
Referencias:
Año: 2002 vol. 530 p. 169 - 173
ISSN:
0014-5793
Resumen:
Abstract In 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 modication
occurred in leaves, where the enzyme is composed by a single
58 kDa polypeptide.GAPN partially puried 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.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.
