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Nat Commun. 2017 Nov 1;8(1):1237. doi: 10.1038/s41467-017-01437-z.

INA complex liaises the F1Fo-ATP synthase membrane motor modules.

Author information

1
Department of Cellular Biochemistry, University Medical Center Göttingen, GZMB, D-37073, Göttingen, Germany.
2
Department of Biochemistry and Functional Proteomics, Faculty of Biology, University Freiburg, D-79104, Freiburg, Germany.
3
BIOSS Centre for Biological Signalling Studies, University of Freiburg, D-79104, Freiburg, Germany.
4
Department of Cellular Biochemistry, University Medical Center Göttingen, GZMB, D-37073, Göttingen, Germany. Peter.Rehling@medizin.uni-goettingen.de.
5
Max Planck Institute for Biophysical Chemistry, D-37077, Göttingen, Germany. Peter.Rehling@medizin.uni-goettingen.de.

Abstract

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 F1-portion is built on Atp6/8 and loss of INAC causes accumulation of the free F1. An independent complex is formed between INAC and the Atp9 ring. We conclude that INAC maintains assembly intermediates of the F1 F0-ATP synthase in a primed state for the terminal assembly step-motor module formation.

PMID:
29093463
PMCID:
PMC5665977
DOI:
10.1038/s41467-017-01437-z
[Indexed for MEDLINE]
Free PMC Article

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