کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1949579 | 1537765 | 2011 | 13 صفحه PDF | دانلود رایگان |

Coenzyme Q (ubiquinone or Q) is a lipid electron and proton carrier in the electron transport chain. In yeast Saccharomyces cerevisiae eleven genes, designated COQ1 through COQ9, YAH1 and ARH1, have been identified as being required for Q biosynthesis. One of these genes, COQ8 (ABC1), encodes an atypical protein kinase, containing six (I, II, III, VIB, VII, and VIII) of the twelve motifs characteristically present in canonical protein kinases. Here we characterize seven distinct Q-less coq8 yeast mutants and show that unlike the coq8 null mutant, each maintained normal steady-state levels of the Coq8 polypeptide. The phosphorylation states of Coq polypeptides were determined with two-dimensional gel analyses. Coq3p, Coq5p, and Coq7p were phosphorylated in a Coq8p-dependent manner. Expression of a human homolog of Coq8p, ADCK3(CABC1) bearing an amino-terminal yeast mitochondrial leader sequence, rescued growth of yeast coq8 mutants on medium containing a nonfermentable carbon source and partially restored biosynthesis of Q6. The phosphorylation state of several of the yeast Coq polypeptides was also rescued, indicating a profound conservation of yeast Coq8p and human ADCK3 protein kinase function in Q biosynthesis.
Research highlights
► Yeast coq8 mutants were identified that maintain normal steady-state levels of Coq8p.
► S. cerevisiae Coq8 polypeptide is required for phosphorylation of Coq3, Coq5 and Coq7.
► The human Coq8 homolog ADCK3 expressed in yeast coq8 mutants rescues Q biosynthesis.
► Human ADCK3 rescues phosphorylation of yeast Coq polypeptides in yeast coq8 mutants.
► The results indicate a profound conservation of Coq8/ADCK3 function in Q synthesis.
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1811, Issue 5, May 2011, Pages 348–360