YIL042c and YOR090c encode the kinase and phosphatase of the Saccharomyces cerevisiae pyruvate dehydrogenase complex
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
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.
Details
| Original language | English |
|---|---|
| Pages (from-to) | 2553-60 |
| Number of pages | 8 |
| Journal | FEBS letters |
| Volume | 580 |
| Issue number | 11 |
| Publication status | Published - 15 May 2006 |
| Peer-reviewed | Yes |
External IDs
| Scopus | 33646181563 |
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Keywords
Keywords
- Amino Acid Sequence, Conserved Sequence, Humans, Mitochondria/metabolism, Mitochondrial Proteins/metabolism, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Kinases/chemistry, Protein Serine-Threonine Kinases, Protein Subunits/genetics, Pyruvate Dehydrogenase (Lipoamide)-Phosphatase/chemistry, Pyruvate Dehydrogenase Acetyl-Transferring Kinase, Pyruvate Dehydrogenase Complex/chemistry, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/chemistry, Sequence Alignment, Sequence Homology, Amino Acid