Premium
Pleiotropic phenotypes of fission yeast defective in ubiquinone‐10 production. A study from the abc1Sp (coq8Sp) mutant
Author(s) -
Saiki Ryoichi,
Ogiyama Yuki,
Kainou Tomohiro,
Nishi Tomoko,
Matsuda Hideyuki,
Kawamukai Makoto
Publication year - 2003
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.5520180225
Subject(s) - mutant , schizosaccharomyces pombe , biochemistry , coenzyme q – cytochrome c reductase , phenotype , wild type , biology , biosynthesis , yeast , cofactor , glutathione , chemistry , mitochondrion , gene , enzyme , cytochrome c
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.