English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
There are no MPG-Authors available
Locator
There are no locators available
Fulltext (public)

2496342.pdf
(Publisher version), 2MB

Supplementary Material (public)

2496342_Suppl_1.pdf
(Supplementary material), 7MB

2496342_Suppl_2.pdf
(Supplementary material), 249KB

2496342_Suppl_3.xlsx
(Supplementary material), 55KB

2496342_Suppl_4.xlsx
(Supplementary material), 280KB

2496342_Suppl_5.xlsx
(Supplementary material), 228KB

Citation

Naumenko, N., Morgenstern, M., Rucktäschel, R., Warscheid, B., & Rehling, P. (2017). INA complex liaises the F1Fo-ATP synthase membrane motor modules. Nature Communications, 8: 1237. doi:10.1038/s41467-017-01437-z.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-2699-0
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.