Non‐phosphorylating glyceraldehyde‐3‐phosphate dehydrogenase is post‐translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum)

FEBS Letters

Iglesias, Alberto A¹  Bustos, Diego M¹ 

[1] Instituto Tecnológico de Chascomús (IIB-INTECH), Camino Circunv. Laguna km 6, Casilla de Correo 164, Chascomús 7130, Buenos Aires, Argentina

关键词: Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase;    Post-translational modification;    Enzyme phosphorylation;    Triticum aestivum;    ALDH;    aldehyde dehydrogenase;    Ga3P;    glyceraldehyde-3-phosphate;    GAPC;    NAD-dependent glyceraldehyde-3-phosphate dehydrogenase;    phosphorylating;    GAPN;    non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase;    RACE;    rapid amplification of cDNA ends;   

DOI  :  10.1016/S0014-5793(02)03455-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 different subunits of about 58 and 60 kDa in endosperm and shoots. The latter was attributed to in vivo phosphorylation of shoot GAPN. No modification occurred in leaves, where the enzyme is composed by a single 58 kDa polypeptide. GAPN partially purified from shoots and endosperm was dephosphorylated in vitro with alkaline phosphatase. Phosphorylated GAPN exhibited similar affinity for substrates but a lower V _max compared to the non-phosphorylated enzyme. Results suggest that reversible phosphorylation of GAPN could regulate NADPH production in the cytosol of heterotrophic plant cells.

【 授权许可】

Unknown