期刊
NATURE COMMUNICATIONS
卷 8, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-00359-0
关键词
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资金
- Deutsche Forschungsgemeinschaft
- Excellence Initiative of the German Federal & State Governments [EXC 294 BIOSS]
- RTG [GRK2202]
- Ministerium fur Innovation, Wissenschaft and Forschung des Landes Nordrhein-Westfalen
- Emmy-Noether Programm of the Deutsche Forschungsgemeinschaft
- CAPES Foundation
The mitochondrial proteome comprises similar to 1000 (yeast)-1500 (human) different proteins, which are distributed into four different subcompartments. The sublocalization of these proteins within the organelle in most cases remains poorly defined. Here we describe an integrated approach combining stable isotope labeling, various protein enrichment and extraction strategies and quantitative mass spectrometry to produce a quantitative map of submitochondrial protein distribution in S. cerevisiae. This quantitative landscape enables a proteome-wide classification of 986 proteins into soluble, peripheral, and integral mitochondrial membrane proteins, and the assignment of 818 proteins into the four subcompartments: outer membrane, inner membrane, intermembrane space, or matrix. We also identified 206 proteins that were not previously annotated as localized to mitochondria. Furthermore, the protease Prd1, misannotated as intermembrane space protein, could be re-assigned and characterized as a presequence peptide degrading enzyme in the matrix.
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