The proteome of Saccharomyces cerevisiae mitochondria
Copyright policy )The proteome of Saccharomyces cerevisiae mitochondria
We performed a comprehensive approach to determine the proteome of Saccharomyces cerevisiae mitochondria. The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. From >20 million MS spectra, 750 different proteins were identified, indicating an involvement of mitochondria in numerous cellular processes. All known components of the oxidative phosphorylation machinery, the tricarboxylic acid cycle, and the stable mitochondria-encoded proteins were found. Based on the mitochondrial proteins described in the literature so far, we calculate that the identified proteins represent ≈90% of all mitochondrial proteins. The function of a quarter of the identified proteins is unknown. The mitochondrial proteome will provide an important database for the analysis of new mitochondrial and mitochondria-associated functions and the characterization of mitochondrial diseases.
- University of Göttingen Germany
- University of Freiburg Germany
- Ruhr University Bochum Germany
- University of Würzburg Germany
Proteome, Citric Acid Cycle, Saccharomyces cerevisiae, Mass Spectrometry, Mitochondria, Oxygen, Protein Transport, Databases as Topic, Electrophoresis, Gel, Two-Dimensional, Electrophoresis, Polyacrylamide Gel, Phosphorylation
Proteome, Citric Acid Cycle, Saccharomyces cerevisiae, Mass Spectrometry, Mitochondria, Oxygen, Protein Transport, Databases as Topic, Electrophoresis, Gel, Two-Dimensional, Electrophoresis, Polyacrylamide Gel, Phosphorylation
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