期刊
CELL
卷 139, 期 2, 页码 428-439出版社
CELL PRESS
DOI: 10.1016/j.cell.2009.07.045
关键词
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资金
- Deutsche Forschungsgemeinschaft
- Sonderforschungsbereich 746
- Excellence Initiative of the German Federal and State Governments [EXC 294]
- Gottfried Wilhelm Leibniz Program
- Trinational Research Training Group [GRK 1478]
- Ministerium fur Innovation
- Wissenschaft, Forschung und Technologie des Landes Nordrhein-Westfalen
- Bundesministerium fur Bildung und Forschung
- Fonds der Chemischen Industrie
- Fund for Scientific Research-Flanders (Belgium)
- Ghent University
- Inter University Attraction Poles [IUAP06]
- European Union Interaction Proteome (6th Framework Program)
Many mitochondrial proteins are synthesized with N-terminal presequences that are removed by specific peptidases. The N-termini of the mature proteins and thus peptidase cleavage sites have only been determined for a small fraction of mitochondrial proteins and yielded a controversial situation for the cleavage site specificity of the major mitochondrial processing peptidase (MPP). We report a global analysis of the N-proteome of yeast mitochondria, revealing the N-termini of 615 different proteins. Significantly more proteins than predicted contained cleavable presequences. We identified the intermediate cleaving peptidase Icp55, which removes an amino acid from a characteristic set of MPP-generated N-termini, solving the controversial situation of MPP specificity and suggesting that Icp55 converts instable intermediates into stable proteins. Our results suggest that Icp55 is critical for stabilization of the mitochondrial proteome and illustrate how the N-proteome can serve as rich source for a systematic analysis of mitochondrial protein targeting, cleavage and turnover.
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