Proteomics

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INA complex liaises the F1Fo-ATP synthase membrane motor modules

ABSTRACT: The F1Fo-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 section 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 initially 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 F1Fo-ATP synthase in a primed state for the terminal assembly step – channel and motor module formation.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Friedel Drepper  

LAB HEAD: Prof. Dr. Bettina Warscheid

PROVIDER: PXD006249 | Pride | 2017-11-03

REPOSITORIES: Pride

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Publications

INA complex liaises the F<sub>1</sub>F<sub>o</sub>-ATP synthase membrane motor modules.

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]

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