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


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.

SUBMITTER: Aich A 

PROVIDER: S-EPMC5809144 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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

Aich Abhishek A   Wang Cong C   Chowdhury Arpita A   Ronsör Christin C   Pacheu-Grau David D   Richter-Dennerlein Ricarda R   Dennerlein Sven S   Rehling Peter P  

eLife 20180130


Cytochrome <i>c</i> 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 C  ...[more]

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