INA complex liaises the F1Fo-ATP synthase membrane motor modules

The inner membrane assembly complex (INAC) interacts with components of the F1F0-ATP synthase but its function remains unclear. Here the authors show that INAC associates with two distinct complexes during F1F0-ATP synthase formation, which points towards a safeguarding role during proton-conducting...

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Autores principales:	Nataliia Naumenko, Marcel Morgenstern, Robert Rucktäschel, Bettina Warscheid, Peter Rehling
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/fab469cfe0cf474e93bab6274a6e4024
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id	oai:doaj.org-article:fab469cfe0cf474e93bab6274a6e4024
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spelling	oai:doaj.org-article:fab469cfe0cf474e93bab6274a6e40242021-12-02T14:40:49ZINA complex liaises the F1Fo-ATP synthase membrane motor modules10.1038/s41467-017-01437-z2041-1723https://doaj.org/article/fab469cfe0cf474e93bab6274a6e40242017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01437-zhttps://doaj.org/toc/2041-1723The inner membrane assembly complex (INAC) interacts with components of the F1F0-ATP synthase but its function remains unclear. Here the authors show that INAC associates with two distinct complexes during F1F0-ATP synthase formation, which points towards a safeguarding role during proton-conducting channel assembly.Nataliia NaumenkoMarcel MorgensternRobert RucktäschelBettina WarscheidPeter RehlingNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Nataliia Naumenko Marcel Morgenstern Robert Rucktäschel Bettina Warscheid Peter Rehling INA complex liaises the F1Fo-ATP synthase membrane motor modules
description	The inner membrane assembly complex (INAC) interacts with components of the F1F0-ATP synthase but its function remains unclear. Here the authors show that INAC associates with two distinct complexes during F1F0-ATP synthase formation, which points towards a safeguarding role during proton-conducting channel assembly.
format	article
author	Nataliia Naumenko Marcel Morgenstern Robert Rucktäschel Bettina Warscheid Peter Rehling
author_facet	Nataliia Naumenko Marcel Morgenstern Robert Rucktäschel Bettina Warscheid Peter Rehling
author_sort	Nataliia Naumenko
title	INA complex liaises the F1Fo-ATP synthase membrane motor modules
title_short	INA complex liaises the F1Fo-ATP synthase membrane motor modules
title_full	INA complex liaises the F1Fo-ATP synthase membrane motor modules
title_fullStr	INA complex liaises the F1Fo-ATP synthase membrane motor modules
title_full_unstemmed	INA complex liaises the F1Fo-ATP synthase membrane motor modules
title_sort	ina complex liaises the f1fo-atp synthase membrane motor modules
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/fab469cfe0cf474e93bab6274a6e4024
work_keys_str_mv	AT nataliianaumenko inacomplexliaisesthef1foatpsynthasemembranemotormodules AT marcelmorgenstern inacomplexliaisesthef1foatpsynthasemembranemotormodules AT robertrucktaschel inacomplexliaisesthef1foatpsynthasemembranemotormodules AT bettinawarscheid inacomplexliaisesthef1foatpsynthasemembranemotormodules AT peterrehling inacomplexliaisesthef1foatpsynthasemembranemotormodules
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INA complex liaises the F1Fo-ATP synthase membrane motor modules

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