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Saccharomyces cerevisiae mitoproteome plasticity in response to recombinant alternative ubiquinol oxidase
Grégory Mathy1, Rachel Navet, Pascal Gerkens
1Laboratory of Bioenergetics, Bât. B6c, Allée de la Chimie 3, 4000, Liège, Belgium.
Abstract:
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.
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