Saccharomyces cerevisiaepyruvate kinase Pyk1 is PKA phosphorylation substrate in vitro
Open Access
- 1 September 2001
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 203 (2) , 223-227
- https://doi.org/10.1111/j.1574-6968.2001.tb10845.x
Abstract
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-Bcy1 antibodies. Yeast pyruvate kinase Pyk1 identified by amino acid microsequencing analysis and immunoblotting with anti-Pyk1 antibodies copurified with the PKA-1 but not the -2 fraction. Pyk1 can be phosphorylated by yeast PKA in vitro in the presence of cAMP and cGMP. Two-dimensional gel electrophoretic analysis revealed four phosphorylated forms of Pyk1 modified by PKA. In phosphorylation of Pyk1 mainly the Tpk2 catalytic subunit of yeast PKA was involved.Keywords
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