The proteome of Saccharomyces cerevisiae mitochondria
Autor: | Cornelia Joppich, Jörg Reinders, Yvonne Wagner, Agnieszka Chacinska, Chris Meisinger, Birgit Schönfisch, Peter Rehling, Inge Perschil, Bernard Guiard, Nikolaus Pfanner, René P. Zahedi, Albert Sickmann, Helmut E. Meyer |
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Rok vydání: | 2003 |
Předmět: |
Multidisciplinary
Proteome biology Citric Acid Cycle Saccharomyces cerevisiae Oxidative phosphorylation Biological Sciences Mitochondrion biology.organism_classification Mass Spectrometry Yeast Mitochondria Oxygen Citric acid cycle Protein Transport Databases as Topic Biochemistry Electrophoresis Gel Two-Dimensional Electrophoresis Polyacrylamide Gel Phosphorylation Function (biology) Sorting and assembly machinery |
Zdroj: | Proceedings of the National Academy of Sciences. 100:13207-13212 |
ISSN: | 1091-6490 0027-8424 |
DOI: | 10.1073/pnas.2135385100 |
Popis: | 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. |
Databáze: | OpenAIRE |
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