Mapping protein interactions in the active TOM-TIM23 supercomplex

The TOM and TIM23 complexes facilitate the transport of nuclear-encoded proteins into the mitochondrial matrix. Here, the authors use a stalled client protein to purify the translocation supercomplex and gain insight into the TOM-TIM23 interface and the mechanism of protein handover from the TOM to...

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Autores principales:	Ridhima Gomkale, Andreas Linden, Piotr Neumann, Alexander Benjamin Schendzielorz, Stefan Stoldt, Olexandr Dybkov, Markus Kilisch, Christian Schulz, Luis Daniel Cruz-Zaragoza, Blanche Schwappach, Ralf Ficner, Stefan Jakobs, Henning Urlaub, Peter Rehling
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8744caceb7e7478892fe2e26b0cf2134
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spelling	oai:doaj.org-article:8744caceb7e7478892fe2e26b0cf21342021-12-02T17:18:17ZMapping protein interactions in the active TOM-TIM23 supercomplex10.1038/s41467-021-26016-12041-1723https://doaj.org/article/8744caceb7e7478892fe2e26b0cf21342021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26016-1https://doaj.org/toc/2041-1723The TOM and TIM23 complexes facilitate the transport of nuclear-encoded proteins into the mitochondrial matrix. Here, the authors use a stalled client protein to purify the translocation supercomplex and gain insight into the TOM-TIM23 interface and the mechanism of protein handover from the TOM to the TIM23 complex.Ridhima GomkaleAndreas LindenPiotr NeumannAlexander Benjamin SchendzielorzStefan StoldtOlexandr DybkovMarkus KilischChristian SchulzLuis Daniel Cruz-ZaragozaBlanche SchwappachRalf FicnerStefan JakobsHenning UrlaubPeter RehlingNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ridhima Gomkale Andreas Linden Piotr Neumann Alexander Benjamin Schendzielorz Stefan Stoldt Olexandr Dybkov Markus Kilisch Christian Schulz Luis Daniel Cruz-Zaragoza Blanche Schwappach Ralf Ficner Stefan Jakobs Henning Urlaub Peter Rehling Mapping protein interactions in the active TOM-TIM23 supercomplex
description	The TOM and TIM23 complexes facilitate the transport of nuclear-encoded proteins into the mitochondrial matrix. Here, the authors use a stalled client protein to purify the translocation supercomplex and gain insight into the TOM-TIM23 interface and the mechanism of protein handover from the TOM to the TIM23 complex.
format	article
author	Ridhima Gomkale Andreas Linden Piotr Neumann Alexander Benjamin Schendzielorz Stefan Stoldt Olexandr Dybkov Markus Kilisch Christian Schulz Luis Daniel Cruz-Zaragoza Blanche Schwappach Ralf Ficner Stefan Jakobs Henning Urlaub Peter Rehling
author_facet	Ridhima Gomkale Andreas Linden Piotr Neumann Alexander Benjamin Schendzielorz Stefan Stoldt Olexandr Dybkov Markus Kilisch Christian Schulz Luis Daniel Cruz-Zaragoza Blanche Schwappach Ralf Ficner Stefan Jakobs Henning Urlaub Peter Rehling
author_sort	Ridhima Gomkale
title	Mapping protein interactions in the active TOM-TIM23 supercomplex
title_short	Mapping protein interactions in the active TOM-TIM23 supercomplex
title_full	Mapping protein interactions in the active TOM-TIM23 supercomplex
title_fullStr	Mapping protein interactions in the active TOM-TIM23 supercomplex
title_full_unstemmed	Mapping protein interactions in the active TOM-TIM23 supercomplex
title_sort	mapping protein interactions in the active tom-tim23 supercomplex
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/8744caceb7e7478892fe2e26b0cf2134
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Mapping protein interactions in the active TOM-TIM23 supercomplex

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