Krause-Buchholz Udo, Gey Uta, Wünschmann Jana, Becker Susanne, Rödel Gerhard
Institut für Genetik, Technische Universität Dresden, 01062 Dresden, Germany.
FEBS Lett. 2006 May 15;580(11):2553-60. doi: 10.1016/j.febslet.2006.04.002. Epub 2006 Apr 12.
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.
在酿酒酵母中，丙酮酸脱氢酶（PDH）复合体通过其Pda1p亚基的可逆磷酸化进行调节。我们在此提供证据表明，Pda1p由线粒体激酶Yil042cp磷酸化。编码一种假定的线粒体磷酸酶的YOR090c基因缺失会导致PDH活性降低，这表明Yor090cp作为相应的PDH磷酸酶发挥作用。我们通过蓝色非变性凝胶电泳和串联亲和纯化证明，这两种酶都与PDH复合体相关。
