Catalases protect cellular proteins from oxidative modification in Saccharomyces cerevisiae

Cell Biol Int. 2005 Mar;29(3):187-92. doi: 10.1016/j.cellbi.2004.11.001.

Abstract

The yeast Saccharomyces cerevisiae cells had higher antioxidant enzyme activities under growth in ethanol than that in glucose as a carbon and energy source. The correlations between catalase activity and protein carbonyl level (r(2)=0.857), between catalase and glucose-6-phosphate dehydrogenase activities (r(2)=0.924) and between protein carbonyl levels and glucose-6-phosphate dehydrogenase activity (r(2)=0.988) under growth in ethanol were found. Growing in ethanol the strain deficient in cytosolic and peroxisomal catalases had 7.1-fold higher level of carbonyl proteins than that of wild-type strain. Our data suggest that in vivo catalases may protect glucose-6-phosphate dehydrogenase against oxidative inactivation.

MeSH terms

  • Antioxidants / metabolism
  • Catalase / physiology*
  • Cytosol / drug effects
  • Cytosol / enzymology
  • Ethanol / pharmacology
  • Glucose / pharmacology
  • Glucosephosphate Dehydrogenase / metabolism*
  • Glutathione Reductase / metabolism*
  • Oxidation-Reduction
  • Oxidative Stress*
  • Peroxisomes / drug effects
  • Peroxisomes / enzymology
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / growth & development*
  • Superoxide Dismutase / metabolism*

Substances

  • Antioxidants
  • Ethanol
  • Glucosephosphate Dehydrogenase
  • Catalase
  • Superoxide Dismutase
  • Glutathione Reductase
  • Glucose