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FEBS Lett. 1995 Oct 9;373(2):111-4.

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

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  • 1Division of Biochemistry and Molecular Biology, University of Glasgow, Scotland, UK.


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.

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