COX16 promotes COX2 metallation and assembly during respiratory complex IV biogenesis
2018 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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- Authors
- Aich, Abhishek; Wang, Cong; Chowdhury, Arpita; Ronsör, Christin; Pacheu-Grau, David; Richter-Dennerlein, Ricarda ; Dennerlein, Sven; Rehling, Peter
- 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.
- Issue Date
- 2018
- Journal
- eLife
- Project
- SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz
SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien - Organization
- Universitätsmedizin Göttingen
- Working Group
- RG Rehling (Mitochondrial Protein Biogenesis)
- ISSN
- 2050-084X
- Language
- English