Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-017-01437-z
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Funding
- Deutsche Forschungsgemeinschaft [PR1384/52, SFB860, EXC 294 BIOSS]
- European Research Council (ERC) Consolidator Grant [648235]
- Max Planck Society (PR)
- Ph.D. program Molecular Biology-International Max Planck Research School
- Gottingen Graduate School for Neurosciences and Molecular Biosciences (GGNB
- DFG Grant) [GSC 226/1]
- European Research Council (ERC) [648235] Funding Source: European Research Council (ERC)
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The F1F0-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex's membrane-embedded motor forms a proteinaceous channel at the interface between Atp9 ring and Atp6. To prevent unrestricted proton flow dissipating the H+-gradient, channel formation is a critical and tightly controlled step during ATP synthase assembly. Here we show that the INA complex (INAC) acts at this decisive step promoting Atp9-ring association with Atp6. INAC binds to newly synthesized mitochondrial-encoded Atp6 and Atp8 in complex with maturation factors. INAC association is retained until the F-1-portion is built on Atp6/8 and loss of INAC causes accumulation of the free F-1. An independent complex is formed between INAC and the Atp9 ring. We conclude that INAC maintains assembly intermediates of the F1F0-ATP synthase in a primed state for the terminal assembly step-motor module formation.
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