Gey Uta, Czupalla Cornelia, Hoflack Bernard, Rödel Gerhard, Krause-Buchholz Udo
Institute of Genetics, Dresden University of Technology, 01062 Dresden, Germany.
J Biol Chem. 2008 Apr 11;283(15):9759-67. doi: 10.1074/jbc.M708779200. Epub 2008 Jan 7.
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 alpha-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.
酵母丙酮酸脱氢酶复合体的活性受可逆磷酸化作用调控。最近我们鉴定出了两种参与丙酮酸脱氢酶复合体α亚基Pda1p磷酸化（Pkp1p）和去磷酸化（Ppp1p）过程的酶。在此我们提供证据表明，另外两种线粒体蛋白Pkp2p（Ygl059wp）和Ppp2p（Ycr079wp）通过影响Pda1p的磷酸化状态参与该复合体的调控。我们的数据表明激酶具有互补活性，而磷酸酶具有冗余功能。这两种蛋白都与该复合体相关联。我们提出了一个关于调控酶的作用以及Pda1p的磷酸化状态在丙酮酸脱氢酶复合体组装过程中的作用的模型。
