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Issue title: The Third Conference of the International CoQ10 Association
Article type: Research Article
Authors: Saiki, Ryoichi | Ogiyama, Yuki | Kainou, Tomohiro | Nishi, Tomoko | Matsuda, Hideyuki | Kawamukai, Makoto
Affiliations: Faculty of Life and Environmental Science, Shimane University, 1060 Nishikawatsu, Matsue, 690-8504, Japan
Note: [] Corresponding author: Fax: +81 852 32 6049; E-mail: kawamuka@life.shimane-u.ac.jp
Abstract: We previously constructed two Schizosaccahromyces pombe ubiquinone-10 (or Coenzyme Q_{10}) less mutants, which are either defective for decaprenyl diphosphate synthase or p-hydroxybenzoate polyprenyl diphosphate transferase. To further confirm the roles of ubiquinone in S. pombe, we examined the phenotype of the abc1Sp (coq8Sp) mutant, which is highly speculated to be defective in ubiquinone biosynthesis. We show here that the abc1Sp defective strain did not produce UQ-10 and could not grow on minimal medium. The abc1Sp-deficient strain required supplementation with antioxidants such as cysteine or glutathione to grow on minimal medium. In support of the antioxidant function of ubiquinone, the abc1Sp-deficient strain is sensitive to H_{2}O_{2} and Cu^{2+}. In addition, expression of the stress inducible ctt1 gene was much induced in the ubiquinone less mutant than wild type. Interestingly, we also found that the abc1-deficient strain as well as other ubiquinone less mutants produced a significant amount of H_{2}S, which suggests that oxidation of sulfide by ubiquinone may be an important pathway for sulfur metabolism in S. pombe. Thus, analysis of the phenotypes of S. pombe ubiquinone less mutants clearly demonstrate that ubiquinone has multiple functions in the cell apart from being an integral component of the electron transfer system.
Keywords: fission yeast, ubiquinone-10, antioxidant, sulfide, coq8
Journal: BioFactors, vol. 18, no. 1-4, pp. 229-235, 2003
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