Purification and characterization of Ag,Zn-superoxide dismutase from Saccharomyces cerevisiae exposed to silver

J Biol Chem. 1994 Oct 14;269(41):25783-7.

Abstract

Cu,Zn-superoxide dismutase plays an important role in protecting cells from oxygen toxicity by catalyzing the dismutation of superoxide anion into hydrogen peroxide and oxygen. In Saccharomyces cerevisiae Cu,Zn-superoxide dismutase is coregulated with copper-thionein by copper via the transcription factor ACE 1. We demonstrate here that presence of AgNO3 in the culture medium leads to a five times increase of Cu,Zn-superoxide dismutase mRNA, with a concomitant six times decrease of the enzyme activity. Susceptibility of yeast to silver was apparently inversely related to Cu,Zn-superoxide dismutase activity. From silver-treated yeast a Cu,Zn-superoxide dismutase with impaired dismutase function was purified and was shown to contain silver, which was located to the copper site. These data suggest that Cu,Zn-superoxide dismutase may play an additional direct role in the defense of S. cerevisiae against metal stress by functioning as metal chelator.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Division / drug effects
  • Electron Spin Resonance Spectroscopy
  • Gene Expression Regulation, Fungal
  • Isoelectric Focusing
  • RNA, Messenger / analysis
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / growth & development
  • Silver Nitrate / metabolism*
  • Silver Nitrate / pharmacology
  • Structure-Activity Relationship
  • Superoxide Dismutase / chemistry*
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / isolation & purification
  • Superoxide Dismutase / metabolism

Substances

  • RNA, Messenger
  • Silver Nitrate
  • Superoxide Dismutase