Journal
CELL METABOLISM
Volume 16, Issue 4, Pages 538-549Publisher
CELL PRESS
DOI: 10.1016/j.cmet.2012.08.009
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Funding
- Deutsche Forschungsgemeinschaft [SFB815]
- BMBF [0315584A: GerontoMitoSys, 01GM1113B: mitoNET]
- Excellence Initiative of the German Federal Government [EXC 115]
- Excellence Initiative of the German State Government [EXC 115]
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Macromolecular complexes are essential players in numerous biological processes. They are often large, dynamic, and rather labile; approaches to study them are scarce. Covering masses up to similar to 30 MDa, we separated the native complexome of rat heart mitochondria by blue-native and large-pore blue-native gel electrophoresis to analyze its constituents by mass spectrometry. Similarities in migration patterns allowed hierarchical clustering into interaction profiles representing a comprehensive analysis of soluble and membrane-bound complexes of an entire organelle. The power of this bottom-up approach was validated with well-characterized mitochondrial multiprotein complexes. TMEM126B was found to comigrate with known assembly factors of mitochondrial complex I, namely CIA30, Ecsit, and Acad9. We propose terming this complex mitochondria! complex I assembly (MCIA) complex. Furthermore, we demonstrate that TMEM126B is required for assembly of complex I. In summary, complexome profiling is a powerful and unbiased technique allowing the identification of previously overlooked components of large multiprotein complexes.
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