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Heide, Heinrich; Bleier, Lea; Steger, Mirco; Ackermann, Jörg; Dröse, Stefan; Schwamb, Bettina; Zörnig, Martin; Reichert, Andreas S.; Koch, Ina; Wittig, Ilka; Brandt, Ulrich
Cell metabolism, 10/2012, Letnik: 16, Številka: 4Journal Article
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 ∼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 mitochondrial 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. Display omitted ► Multiprotein complexes up to a mass of 30 MDa are analyzed by proteomic profiling ► The power of complexome profiling is shown for mitochondrial multiprotein complexes ► TMEM126B is essential for the assembly of mitochondrial complex I ► TMEM126B is a subunit of the mitochondrial complex I assembly (MCIA) complex
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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