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  COX16 promotes COX2 metallation and assembly during respiratory complex IV biogenesis.

Aich, A., Wang, C., Chowdhury, A., Ronsör, C., Pacheu-Grau, D., Richter-Dennerlein, R., et al. (2018). COX16 promotes COX2 metallation and assembly during respiratory complex IV biogenesis. eLife, 7: e32572. doi:10.7554/eLife.32572.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-B358-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-1A9D-0
Genre: Journal Article

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 Creators:
Aich, A., Author
Wang, C., Author
Chowdhury, A., Author
Ronsör, C., Author
Pacheu-Grau, D., Author
Richter-Dennerlein, R., Author
Dennerlein, S., Author
Rehling, P.1, Author              
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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 Abstract: Cytochrome c oxidase of the mitochondrial oxidative phosphorylation system reduces molecular oxygen with redox equivalent-derived electrons. The conserved mitochondrial-encoded COX1- and COX2-subunits are the heme- and copper-center containing core subunits that catalyze water formation. COX1 and COX2 initially follow independent biogenesis pathways creating assembly modules with subunit-specific, chaperone-like assembly factors that assist in redox centers formation. Here, we find that COX16, a protein required for cytochrome c oxidase assembly, interacts specifically with newly synthesized COX2 and its copper center-forming metallochaperones SCO1, SCO2, and COA6. The recruitment of SCO1 to the COX2-module is COX16- dependent and patient-mimicking mutations in SCO1 affect interaction with COX16. These findings implicate COX16 in CuA-site formation. Surprisingly, COX16 is also found in COX1-containing assembly intermediates and COX2 recruitment to COX1. We conclude that COX16 participates in merging the COX1 and COX2 assembly lines.

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Language(s): eng - English
 Dates: 2018-01-30
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.32572
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Title: eLife
Source Genre: Journal
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Pages: 18 Volume / Issue: 7 Sequence Number: e32572 Start / End Page: - Identifier: -