Saccharomyces cerevisiae mitoproteome plasticity in response to recombinant alternative ubiquinol oxidase

J Proteome Res. 2006 Feb;5(2):339-48. doi: 10.1021/pr050346e.


The energy-dissipating alternative oxidase (AOX) from Hansenula anomala was expressed in Saccharomyces cerevisiae. The recombinant AOX was functional. A comparative analysis by two-dimensional differential in-gel electrophoresis (2D-DIGE) of mitochondrial protein patterns found in wild-type and recombinant AOX strains was performed. 60 proteins exhibiting a significant difference in their abundance were identified. Interestingly, proteins implicated in major metabolic pathways such as Krebs cycle and amino acid biosynthesis were up-regulated. Surprisingly, an up-regulation of the respiratory-chain complex III was associated with a down-regulation of the ATP synthase complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electrophoresis, Gel, Two-Dimensional
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Gene Expression Regulation, Fungal*
  • Mass Spectrometry
  • Mitochondria / metabolism*
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Oxygen Consumption
  • Pichia / enzymology
  • Pichia / genetics
  • Plant Proteins
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics


  • Fungal Proteins
  • Mitochondrial Proteins
  • Plant Proteins
  • Recombinant Proteins
  • Oxidoreductases
  • alternative oxidase