Mitochondrial AAA-type protease Yme1p is involved in Bax effects on cytochrome c oxidase

Biochem Biophys Res Commun. 2001 Dec 21;289(5):1314-9. doi: 10.1006/bbrc.2001.6120.

Abstract

Expression of the pro-apoptotic protein Bax in yeast Saccharomyces cerevisiae induces a release of cytochrome c accompanied by a decrease of the amount of cytochrome c oxidase. Here we show that the decrease of cytochrome c oxidase is due to the activation of mitochondrial protease Yme1p, of which cytochrome c oxidase subunit 2 (Cox2p) is a substrate. The absence of Yme1p slightly delays Bax-induced cell death, suggesting a role of this protease in yeast cell death and thus of its mammalian homologue in apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Dependent Proteases
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism*
  • Apoptosis / physiology
  • Cell Respiration
  • Electron Transport Complex IV / metabolism*
  • Genes, Fungal
  • Genes, myc
  • Humans
  • In Vitro Techniques
  • Mitochondria / enzymology
  • Phenotype
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-bcl-2*
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • bcl-2-Associated X Protein

Substances

  • BAX protein, human
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Saccharomyces cerevisiae Proteins
  • bcl-2-Associated X Protein
  • Electron Transport Complex IV
  • ATP-Dependent Proteases
  • YME1 protein, S cerevisiae
  • Adenosine Triphosphatases