酿酒酵母的丙酮酸脱氢酶复合体受磷酸化作用调控。

The pyruvate dehydrogenase complex of Saccharomyces cerevisiae is regulated by phosphorylation.

作者信息

James A G, Cook R M, West S M, Lindsay J G

机构信息

Division of Biochemistry and Molecular Biology, University of Glasgow, Scotland, UK.

出版信息

FEBS Lett. 1995 Oct 9;373(2):111-4. doi: 10.1016/0014-5793(95)01020-f.

DOI:10.1016/0014-5793(95)01020-f

PMID:7589446

Abstract

Mitochondria were isolated from Saccharomyces cerevisiae grown on different carbon sources prior to incubation with [gamma-32P]ATP. A major 46,000-M(r) phosphoprotein, corresponding in M(r) value to the E1 alpha 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.

摘要

在用[γ-32P]ATP孵育之前，从在不同碳源上生长的酿酒酵母中分离出线粒体。仅在从在可发酵碳源（如半乳糖）上生长的细胞中分离出的线粒体中检测到一种主要的46,000-M（r）磷蛋白，其M（r）值与酵母丙酮酸脱氢酶复合物（PDC）的E1α亚基相对应。用针对哺乳动物或酵母PDC的E1成分的亚基特异性抗血清进行免疫沉淀，证实了该多肽的身份。分离的酵母线粒体中的PDC活性可以以ATP依赖的方式失活，并在Ca2+离子存在下重新激活。