The pyruvate dehydrogenase complex of Saccharomyces cerevisiae is regulated by phosphorylation

FEBS Letters

West, Shauna M.¹  Lindsay, J.Gordon¹  Cook, Ritchard M.¹  James, A.Gordon¹ 

[1] Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, UK

关键词: Yeast;    Pyruvate dehydrogenase complex;    Phosphorylation;    Inactivation and reactivation;    PDC;    pyruvate dehydrogenase complex;    BCOADC;    branched-chain 2-oxoacid dehydrogenase complex;   

DOI  :  10.1016/0014-5793(95)01020-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mitochondria were isolated from Saccharomyces cerevisiae grown on different carbon sources prior to incubation with [γ-³²P]ATP. A major 46,000-M_r phosphoprotein, corresponding in M_r value to the El α subunit of the yeast pyruvate dehydrogenase complex (PDC), was detected only in mitochondria isolated from cells grown on a fermentable carbon source such as galactose. Immunoprecipitation with subunit-specific antiserum to the E1 component of mammalian or yeast PDC confirmed the identity of this polypeptide. PDC activity in isolated yeast mitochondria could be inactivated in an ATP-dependent fashion and reactivated in the presence of Ca²⁺ ions.

【 授权许可】

Unknown