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 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.
Rudolf-Virchow-Center for Experimental Biomedicine, Universität Würzburg, Versbacher Strasse 9, D-97078 Würzburg, Germany.
Albert
A
Sickmann
Jörg
J
Reinders
Yvonne
Y
Wagner
Cornelia
C
Joppich
René
R
Zahedi
Helmut E
HE
Meyer
Birgit
B
Schönfisch
Inge
I
Perschil
Agnieszka
A
Chacinska
Bernard
B
Guiard
Peter
P
Rehling
Nikolaus
N
Pfanner
Chris
C
Meisinger
D002952:Citric Acid Cycle; D019992:Databases as Topic; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry / Q000379:methods; D008928:Mitochondria / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism; D010766:Phosphorylation; D021381:Protein Transport; D020543:Proteome; D012441:Saccharomyces cerevisiae / Q000378:metabolism*
D020543:Proteome; D010100:Oxygen