期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 18, 页码 5685-5690出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1424353112
关键词
assembly; metal protein; FeS cluster; NDUFAF2; NDUFA12
资金
- Deutsche Forschungsgemeinschaft [ZI 552/3-1]
- Excellence Initiative of the German Federal Government [EXC 115, EXC 294 BIOSS]
- Excellence Initiative of the German State Government [EXC 115, EXC 294 BIOSS]
- Humboldt Foundation
Mitochondrial proton-pumping NADH: ubiquinone oxidoreductase (respiratory complex I) comprises more than 40 polypeptides and contains eight canonical FeS clusters. The integration of subunits and insertion of cofactors into the nascent complex is a complicated multistep process that is aided by assembly factors. We show that the accessory NUMM subunit of complex I (human NDUFS6) harbors a Zn-binding site and resolve its position by X-ray crystallography. Chromosomal deletion of the NUMM gene or mutation of Zn-binding residues blocked a late step of complex I assembly. An accumulating assembly intermediate lacked accessory subunit N7BM (NDUFA12), whereas a paralog of this subunit, the assembly factor N7BML (NDUFAF2), was found firmly bound instead. EPR spectroscopic analysis and metal content determination after chromatographic purification of the assembly intermediate showed that NUMM is required for insertion or stabilization of FeS cluster N4.
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