Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052871 | FEBS Letters | 2006 | 8 Pages |
Abstract
In Saccharomyces cerevisiae the pyruvate dehydrogenase (PDH) complex is regulated by reversible phosphorylation of its Pda1p subunit. We here provide evidence that Pda1p is phosphorylated by the mitochondrial kinase Yil042cp. Deletion of YOR090c, encoding a putative mitochondrial phosphatase, results in a decreased PDH activity, indicating that Yor090cp acts as the corresponding PDH phosphatase. We demonstrate by means of blue native gel electrophoresis and tandem affinity purification that both enzymes are associated with the PDH complex.
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Authors
Udo Krause-Buchholz, Uta Gey, Jana Wünschmann, Susanne Becker, Gerhard Rödel,