Ontology highlight
ABSTRACT:
SUBMITTER: Naumenko N
PROVIDER: S-EPMC5665977 | biostudies-literature | 2017 Nov
REPOSITORIES: biostudies-literature
Naumenko Nataliia N Morgenstern Marcel M Rucktäschel Robert R Warscheid Bettina B Rehling Peter P
Nature communications 20171101 1
The F<sub>1</sub>F<sub>0</sub>-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<sup>+</sup>-gradient, channel formation is a critical and tightly controlled step during ATP synthase assembly. Here we show that the INA ...[more]