Abstract
Coenzyme Q (ubiquinone or Q) is a lipid electron carrier in the electron transport chain. In yeast Saccharomyces cerevisiae nine genes, designated COQ1 through COQ9, have been identified as being required for Q biosynthesis. One of these genes, ABC1/COQ8, is now thought to function as a kinase (Tauche et al., 2009). We have characterized seven independent abc1/coq8 mutants (Tzagoloff and Dieckmann, 1990); four contain mutations in kinase subdomains, and three are in uncharacterized motifs. In this study, phosphorylation of Coq3p, Coq5p, and Coq7p are dependent on Coq8p as determined by 2D‐IEF/SDS‐PAGE analyses, while Coq1p was discovered to be highly phosphorylated, but in a less Coq8p‐dependent manner. ADCK3, a human homolog of yeast ABC1/COQ8, was able to restore growth of yeast abc1/coq8 mutants on medium containing a non‐fermentable carbon source. Expression of the human ADCK3 polypeptide in three distinct coq8 yeast mutants increased steady state levels of yeast Coq4p and Coq7p, and restored phosphorylation of Coq3p, Coq5p, and Coq7p. This work is supported in part by National Institutes of Health (NIH) Grant GM45952.
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