Transcription of Schizosaccharomyces pombe thioltransferase-1 in response to stress conditions

J Biochem Mol Biol. 2002 Jul 31;35(4):409-13. doi: 10.5483/bmbrep.2002.35.4.409.

Abstract

Thioltransferase, also known as glutaredoxin, is an enzyme that catalyzes the reduction of a variety of disulfide compounds. In Schizosaccharomyces pombe, two thioltransferases were reported and the cDNA of one of the thioltransferases (thioltransferase-1) was cloned. Using a Northern blot assay, we investigated the thioltransferase transcription in response to various stress conditions. When the culture was shifted to a high temperature, the thioltransferase transcription was not significantly changed compared to the unshifted 30 degrees culture. Treatment of zinc chloride to exponentially-growing cells remarkably increased the thioltransferase transcription, whereas the treatment of mercury chloride greatly reduced the transcription. Treatment of hydrogen peroxide and cadmium chloride caused no significant effects on the transcription of the thioltransferase. These results suggest that the transcription of thioltransferase-1 in S. pombe is induced in response to metal stress that is caused by zinc chloride, but not in response to heat stress or oxidative stress that is caused by hydrogen peroxide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chlorides / pharmacology
  • Glutaredoxins
  • Hot Temperature
  • Hydrogen Peroxide / pharmacology
  • Oxidative Stress
  • Oxidoreductases / genetics*
  • Protein Disulfide Reductase (Glutathione)*
  • Schizosaccharomyces / drug effects
  • Schizosaccharomyces / enzymology*
  • Schizosaccharomyces / genetics*
  • Schizosaccharomyces pombe Proteins / genetics*
  • Transcription, Genetic / drug effects
  • Zinc Compounds / pharmacology

Substances

  • Chlorides
  • Glutaredoxins
  • Schizosaccharomyces pombe Proteins
  • Zinc Compounds
  • zinc chloride
  • Hydrogen Peroxide
  • Oxidoreductases
  • Protein Disulfide Reductase (Glutathione)