Stability and refractoriness of the high catalase activity in the oxidative-stress-resistant fission yeast Schizosaccharomyces pombe
Language English Country United States Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
9821290
DOI
10.1007/bf02818575
Knihovny.cz E-resources
- MeSH
- Aerobiosis MeSH
- Anaerobiosis MeSH
- Cycloheximide pharmacology MeSH
- Ethanol metabolism MeSH
- Glucose metabolism MeSH
- Protein Synthesis Inhibitors pharmacology MeSH
- Catalase metabolism MeSH
- Oxidative Stress * MeSH
- Saccharomyces cerevisiae enzymology growth & development MeSH
- Schizosaccharomyces enzymology growth & development MeSH
- Enzyme Stability MeSH
- Water MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Cycloheximide MeSH
- Ethanol MeSH
- Glucose MeSH
- Protein Synthesis Inhibitors MeSH
- Catalase MeSH
- Water MeSH
Effect of oxygen and metabolic substrates (glucose, ethanol) on the catalase activity of anaerobically grown Schizosaccharomyces pombe cells was assessed and compared with that of Saccharomyces cerevisiae in order to determine the catalase activity regulation in S. pombe. In contrast to S. cerevisiae, the total catalase activity of permeabilized S. pombe anaerobically grown cells is higher than that found in aerobically grown cells, is stable and constant under all circumstances (i.e. it is not induced by oxygen and/or substrates), and only a negligible part (3-5%) of it is contributed by de novo protein synthesis during aeration with or without substrates. The patent catalase activity of intact cells rises 2-fold during 6-h aeration without substrate and 7-8-fold in the presence of glucose or ethanol. The increase is not inhibited by cycloheximide and is thus not due to de novo catalase synthesis, but may reflect enhanced transport of catalase to the cell surface or a permeabilization of the plasma membrane during the aeration.
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