Assembly factors for the membrane arm of human complex I.

TitleAssembly factors for the membrane arm of human complex I.
Publication TypeJournal Article
Year of Publication2013
AuthorsAndrews, B, Carroll, J, Ding, S, Fearnley, IM, Walker, JE
JournalProc Natl Acad Sci U S A
Date Published2013 Nov 19
KeywordsBlotting, Western, Cell Line, Tumor, Electron Transport Complex I, Electrophoresis, Polyacrylamide Gel, Gene Expression Regulation, Humans, Mass Spectrometry, Membrane Proteins, Microscopy, Confocal, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Oxygen Consumption, Protein Multimerization

Mitochondrial respiratory complex I is a product of both the nuclear and mitochondrial genomes. The integration of seven subunits encoded in mitochondrial DNA into the inner membrane, their association with 14 nuclear-encoded membrane subunits, the construction of the extrinsic arm from 23 additional nuclear-encoded proteins, iron-sulfur clusters, and flavin mononucleotide cofactor require the participation of assembly factors. Some are intrinsic to the complex, whereas others participate transiently. The suppression of the expression of the NDUFA11 subunit of complex I disrupted the assembly of the complex, and subcomplexes with masses of 550 and 815 kDa accumulated. Eight of the known extrinsic assembly factors plus a hydrophobic protein, C3orf1, were associated with the subcomplexes. The characteristics of C3orf1, of another assembly factor, TMEM126B, and of NDUFA11 suggest that they all participate in constructing the membrane arm of complex I.

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
Citation Key10.1073/pnas.1319247110
PubMed ID24191001
PubMed Central IDPMC3839705
Grant ListMC_U105663148 / / Medical Research Council / United Kingdom