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J. Biol. Chem., Vol. 283, Issue 15, 9759-9767, April 11, 2008

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Yeast Pyruvate Dehydrogenase Complex Is Regulated by a Concerted Activity of Two Kinases and Two Phosphatases^*

Uta Gey, Cornelia Czupalla, Bernard Hoflack, Gerhard Rödel, and Udo Krause-Buchholz¹

From the Institute of Genetics, Dresden University of Technology, 01062 Dresden, Germany and Biotechnology Center, Dresden University of Technology, Tatzberg 47-51, 01307 Dresden, Germany

The activity of yeast pyruvate dehydrogenase complex is regulated by reversible phosphorylation. Recently we identified two enzymes that are involved in the phosphorylation (Pkp1p) and dephosphorylation (Ppp1p) of Pda1p, the -subunit of the pyruvate dehydrogenase complex. Here we provide evidence that two additional mitochondrial proteins, Pkp2p (Ygl059wp) and Ppp2p (Ycr079wp), are engaged in the regulation of this complex by affecting the phosphorylation state of Pda1p. Our data indicate complementary activities of the kinases and a redundant function for the phosphatases. Both proteins are associated with the complex. We propose a model for the role of the regulatory enzymes and the phosphorylation state of Pda1p in the assembly process of the pyruvate dehydrogenase complex.

Received for publication, October 24, 2007 , and in revised form, December 20, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 49-351-46335960; Fax: 49-351-46337725; E-mail: Udo.Krause-Buchholz{at}tu-dresden.de.

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