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.; Dennerlein, S.; Rehling, P.

doi:10.7554/eLife.32572

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

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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.

Cite as: https://hdl.handle.net/21.11116/0000-0000-B358-3

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.