Saccharomyces cerevisiae pyruvate kinase Pyk1 is PKA phosphorylation substrate in vitro

被引：12

作者：

Cytrynska, M ^{[1
]}

Frajnt, M ^{[1
]}

Jakubowicz, T ^{[1
]}

机构：

[1] Marie Curie Sklodowska Univ, Dept Mol Biol, PL-20033 Lublin, Poland

来源：

FEMS MICROBIOLOGY LETTERS | 2001年 / 203卷 / 02期

关键词：

pyruvate kinase; cAMP-dependent protein kinase; Saccharomyces cerevisiae; protein phosphorylation;

D O I：

10.1016/S0378-1097(01)00354-8

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Fractionation of Saccharomyces cerevisiae postribosomal extract on DEAE-cellulose revealed two fractions of cAMP-dependent protein kinase (PKA-1 and PKA-2). The presence of PKA in both fractions was confirmed by immunoblotting with anti-Bey I antibodies. Yeast pyruvate kinase Pyk1 identified by amino acid microsequencing analysis and immunoblotting with anti-Pyk1 antibodies copurified with the PKA-I but not the -2 fraction. Pyk1 can be phosphorylated by yeast PKA in vitro in the presence of cAMP and cGMP. Two-dimensional gel electrophotetic analysis revealed four phosphorylated forms of Pyk1 modified by PKA. In phosphorylation of Pyk1 mainly the Tpk2 catalytic subunit of yeast PKA was involved. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science BN. All rights reserved.

引用

页码：223 / 227

页数：5

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