NDUFA4 Is a Subunit of Complex IV of the Mammalian Electron Transport Chain

The oxidative phosphorylation system is one of the best-characterized metabolic pathways. In mammals, the protein components and X-ray structures are defined for all complexes except complex I. Here, we show that NDUFA4, formerly considered a constituent of NADH Dehydrogenase (CI), is instead a comp...

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Bibliographic Details
Published in:Cell metabolism 2012-09, Vol.16 (3), p.378-386
Main Authors: Balsa, Eduardo, Marco, Ricardo, Perales-Clemente, Ester, Szklarczyk, Radek, Calvo, Enrique, Landázuri, Manuel O., Enríquez, José Antonio
Format: Article
Language:English
Subjects:
Animals
Blotting, Western
Chromatography, Liquid
Electron Transport Complex IV - genetics
Electron Transport Complex IV - metabolism
Electrophoresis
Evolution, Molecular
Fibroblasts - metabolism
HeLa Cells
Humans
Mice
Oxidative Phosphorylation
Protein Subunits - genetics
Tandem Mass Spectrometry
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Summary:The oxidative phosphorylation system is one of the best-characterized metabolic pathways. In mammals, the protein components and X-ray structures are defined for all complexes except complex I. Here, we show that NDUFA4, formerly considered a constituent of NADH Dehydrogenase (CI), is instead a component of the cytochrome c oxidase (CIV). Deletion of NDUFA4 does not perturb CI. Rather, proteomic, genetic, evolutionary, and biochemical analyses reveal that NDUFA4 plays a role in CIV function and biogenesis. The change in the attribution of the NDUFA4 protein requires renaming of the gene and reconsideration of the structure of CIV. Furthermore, NDUFA4 should be considered a candidate gene for CIV rather than CI deficiencies in humans. [Display omitted] ► NDUFA4 physically interacts with complex IV and not with complex I ► Absence of NDUFA4 does not perturb CI but instead reduces CIV amount and activity ► NDUFA4 coevolved with complex IV and not with complex I
ISSN:1550-4131
1932-7420
DOI:10.1016/j.cmet.2012.07.015