| Literature DB >> 14576278 |
Albert Sickmann1, Jörg Reinders, Yvonne Wagner, Cornelia Joppich, René Zahedi, Helmut E Meyer, Birgit Schönfisch, Inge Perschil, Agnieszka Chacinska, Bernard Guiard, Peter Rehling, Nikolaus Pfanner, Chris Meisinger.
Abstract
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 approximately 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.Entities:
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Year: 2003 PMID： 14576278 PMCID： PMC263752 DOI： 10.1073/pnas.2135385100
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205