Machinery for protein sorting and assembly in the mitochondrial outer membrane

Mitochondria contain translocases for the transport of precursor proteins across their outer and inner membranes. It has been assumed that the translocases also mediate the sorting of proteins to their submitochondrial destination. Here we show that the mitochondrial outer membrane contains a separa...

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Bibliographic Details
Published in:Nature (London) 2003-07, Vol.424 (6948), p.565-571
Main Authors: Wiedemann, Nils, Kozjak, Vera, Chacinska, Agnieszka, Schönfisch, Birgit, Rospert, Sabine, Ryan, Michael T, Pfanner, Nikolaus, Meisinger, Chris
Format: Article
Language:English
Subjects:
Biochemistry
Biological and medical sciences
Cell structures and functions
Fundamental and applied biological sciences. Psychology
Gene Deletion
Humanities and Social Sciences
Intracellular Membranes - metabolism
letter
Macromolecular Substances
Membrane Proteins - biosynthesis
Membrane Proteins - deficiency
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Transport Proteins - metabolism
Membranes
Mitochondria - metabolism
Mitochondria and cell respiration
Mitochondrial Membrane Transport Proteins
Molecular and cellular biology
multidisciplinary
Protein Precursors - metabolism
Protein Transport
Proteins
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - biosynthesis
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Science
Science (multidisciplinary)
Topology
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Summary:Mitochondria contain translocases for the transport of precursor proteins across their outer and inner membranes. It has been assumed that the translocases also mediate the sorting of proteins to their submitochondrial destination. Here we show that the mitochondrial outer membrane contains a separate sorting and assembly machinery (SAM) that operates after the translocase of the outer membrane (TOM). Mas37 forms a constituent of the SAM complex. The central role of the SAM complex in the sorting and assembly pathway of outer membrane proteins explains the various pleiotropic functions that have been ascribed to Mas37 (refs 4, 11-15). These results suggest that the TOM complex, which can transport all kinds of mitochondrial precursor proteins, is not sufficient for the correct integration of outer membrane proteins with a complicated topology, and instead transfers precursor proteins to the SAM complex.
ISSN:0028-0836
1476-4687
DOI:10.1038/nature01753