YidC and SecYEG form a heterotetrameric protein translocation channel

Abstract The heterotrimeric SecYEG complex cooperates with YidC to facilitate membrane protein insertion by an unknown mechanism. Here we show that YidC contacts the interior of the SecY channel resulting in a ligand-activated and voltage-dependent complex with distinct ion channel characteristics....

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Autores principales:	Ilie Sachelaru, Lukas Winter, Denis G. Knyazev, Mirjam Zimmermann, Andreas Vogt, Roland Kuttner, Nicole Ollinger, Christine Siligan, Peter Pohl, Hans-Georg Koch
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4a079782df9745798e53ae586a20f9e7
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spelling	oai:doaj.org-article:4a079782df9745798e53ae586a20f9e72021-12-02T11:52:21ZYidC and SecYEG form a heterotetrameric protein translocation channel10.1038/s41598-017-00109-82045-2322https://doaj.org/article/4a079782df9745798e53ae586a20f9e72017-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00109-8https://doaj.org/toc/2045-2322Abstract The heterotrimeric SecYEG complex cooperates with YidC to facilitate membrane protein insertion by an unknown mechanism. Here we show that YidC contacts the interior of the SecY channel resulting in a ligand-activated and voltage-dependent complex with distinct ion channel characteristics. The SecYEG pore diameter decreases from 8 Å to only 5 Å for the YidC-SecYEG pore, indicating a reduction in channel cross-section by YidC intercalation. In the presence of a substrate, YidC relocates to the rim of the pore as indicated by increased pore diameter and loss of YidC crosslinks to the channel interior. Changing the surface charge of the pore by incorporating YidC into the channel wall increases the anion selectivity, and the accompanying change in wall hydrophobicity is liable to alter the partition of helices from the pore into the membrane. This could explain how the exit of transmembrane domains from the SecY channel is facilitated by YidC.Ilie SachelaruLukas WinterDenis G. KnyazevMirjam ZimmermannAndreas VogtRoland KuttnerNicole OllingerChristine SiliganPeter PohlHans-Georg KochNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ilie Sachelaru Lukas Winter Denis G. Knyazev Mirjam Zimmermann Andreas Vogt Roland Kuttner Nicole Ollinger Christine Siligan Peter Pohl Hans-Georg Koch YidC and SecYEG form a heterotetrameric protein translocation channel
description	Abstract The heterotrimeric SecYEG complex cooperates with YidC to facilitate membrane protein insertion by an unknown mechanism. Here we show that YidC contacts the interior of the SecY channel resulting in a ligand-activated and voltage-dependent complex with distinct ion channel characteristics. The SecYEG pore diameter decreases from 8 Å to only 5 Å for the YidC-SecYEG pore, indicating a reduction in channel cross-section by YidC intercalation. In the presence of a substrate, YidC relocates to the rim of the pore as indicated by increased pore diameter and loss of YidC crosslinks to the channel interior. Changing the surface charge of the pore by incorporating YidC into the channel wall increases the anion selectivity, and the accompanying change in wall hydrophobicity is liable to alter the partition of helices from the pore into the membrane. This could explain how the exit of transmembrane domains from the SecY channel is facilitated by YidC.
format	article
author	Ilie Sachelaru Lukas Winter Denis G. Knyazev Mirjam Zimmermann Andreas Vogt Roland Kuttner Nicole Ollinger Christine Siligan Peter Pohl Hans-Georg Koch
author_facet	Ilie Sachelaru Lukas Winter Denis G. Knyazev Mirjam Zimmermann Andreas Vogt Roland Kuttner Nicole Ollinger Christine Siligan Peter Pohl Hans-Georg Koch
author_sort	Ilie Sachelaru
title	YidC and SecYEG form a heterotetrameric protein translocation channel
title_short	YidC and SecYEG form a heterotetrameric protein translocation channel
title_full	YidC and SecYEG form a heterotetrameric protein translocation channel
title_fullStr	YidC and SecYEG form a heterotetrameric protein translocation channel
title_full_unstemmed	YidC and SecYEG form a heterotetrameric protein translocation channel
title_sort	yidc and secyeg form a heterotetrameric protein translocation channel
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/4a079782df9745798e53ae586a20f9e7
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YidC and SecYEG form a heterotetrameric protein translocation channel

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