Phosphorylation of glyoxysomal malate synthase from castor oil seeds Ricinus communis L.

FEBS Letters

Trelease, Richard N.¹  Randall, Douglas D.¹  Yang, Yan-Ping¹ 

[1] Department of Biochemistry, University of Missouri-Columbia, Columbia, MO 65211, USA

关键词: Malate synthase;    Protein phosphorylation;    Glyoxysome;   

DOI  :  10.1016/0014-5793(88)80097-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

When glyoxysomes isolated from endosperm of 3-day germinated Ricinus communis L. seedlings were incubated with [γ-³²P]ATP, phosphorylation of a small number of endogenous glyoxysomal proteins occurrred. A 64 kDa glyoxysomal matrix protein was predominately phosphorylated. Based upon results of immunoprecipitation, 2D-polyacrylamide gel electrophoresis and Western blotting, the 64 kDa phosphorylated protein is identified as the subunit of malate synthase (EC 4.1.3.2). Phosphorylation of malate synthase was completed within 5 min and the amino acid residue phosphorylated was serine. Phosphorylation was inhibited by EDTA, EGTA and NaF, but enhanced by Triton X-100.

【 授权许可】

Unknown