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Pleiotropic phenotypes of fission yeast defective in ubiquinone-10 production. A study from the abc1Sp (coq8Sp) mutant. | LitMetric

AI Article Synopsis

  • Researchers created two mutants of Schizosaccharomyces pombe (a type of yeast) that lack ubiquinone-10 (Coenzyme Q10) due to defects in key enzymes.
  • The abc1Sp mutant, speculated to be unable to synthesize ubiquinone, showed no UQ-10 production and could only grow on minimal media with added antioxidants like cysteine or glutathione.
  • Findings revealed that the abc1Sp strain was sensitive to oxidative stress and produced excess hydrogen sulfide (H2S), indicating that ubiquinone plays multiple roles in cellular functions beyond just being part of the electron transfer system.

Article Abstract

We previously constructed two Schizosaccahromyces pombe ubiquinone-10 (or Coenzyme Q10) 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 H2O2 and Cu2+. 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 H2S, 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.

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Source
http://dx.doi.org/10.1002/biof.5520180225DOI Listing

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