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SecYEG activates GTPases to drive the completion of cotranslational protein targeting
Signal recognition particle (SRP) and its receptor (SR) comprise a highly conserved cellular machine that cotranslationally targets proteins to a protein-conducting channel, the bacterial SecYEG or eukaryotic Sec61p complex, at the target membrane. Whether SecYEG is a passive recipient of the transl...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575545/ https://www.ncbi.nlm.nih.gov/pubmed/23401005 http://dx.doi.org/10.1083/jcb.201208045 |
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author | Akopian, David Dalal, Kush Shen, Kuang Duong, Franck Shan, Shu-ou |
author_facet | Akopian, David Dalal, Kush Shen, Kuang Duong, Franck Shan, Shu-ou |
author_sort | Akopian, David |
collection | PubMed |
description | Signal recognition particle (SRP) and its receptor (SR) comprise a highly conserved cellular machine that cotranslationally targets proteins to a protein-conducting channel, the bacterial SecYEG or eukaryotic Sec61p complex, at the target membrane. Whether SecYEG is a passive recipient of the translating ribosome or actively regulates this targeting machinery remains unclear. Here we show that SecYEG drives conformational changes in the cargo-loaded SRP–SR targeting complex that activate it for GTP hydrolysis and for handover of the translating ribosome. These results provide the first evidence that SecYEG actively drives the efficient delivery and unloading of translating ribosomes at the target membrane. |
format | Online Article Text |
id | pubmed-3575545 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-35755452013-08-18 SecYEG activates GTPases to drive the completion of cotranslational protein targeting Akopian, David Dalal, Kush Shen, Kuang Duong, Franck Shan, Shu-ou J Cell Biol Research Articles Signal recognition particle (SRP) and its receptor (SR) comprise a highly conserved cellular machine that cotranslationally targets proteins to a protein-conducting channel, the bacterial SecYEG or eukaryotic Sec61p complex, at the target membrane. Whether SecYEG is a passive recipient of the translating ribosome or actively regulates this targeting machinery remains unclear. Here we show that SecYEG drives conformational changes in the cargo-loaded SRP–SR targeting complex that activate it for GTP hydrolysis and for handover of the translating ribosome. These results provide the first evidence that SecYEG actively drives the efficient delivery and unloading of translating ribosomes at the target membrane. The Rockefeller University Press 2013-02-18 /pmc/articles/PMC3575545/ /pubmed/23401005 http://dx.doi.org/10.1083/jcb.201208045 Text en © 2013 Akopian et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Akopian, David Dalal, Kush Shen, Kuang Duong, Franck Shan, Shu-ou SecYEG activates GTPases to drive the completion of cotranslational protein targeting |
title | SecYEG activates GTPases to drive the completion of cotranslational protein targeting |
title_full | SecYEG activates GTPases to drive the completion of cotranslational protein targeting |
title_fullStr | SecYEG activates GTPases to drive the completion of cotranslational protein targeting |
title_full_unstemmed | SecYEG activates GTPases to drive the completion of cotranslational protein targeting |
title_short | SecYEG activates GTPases to drive the completion of cotranslational protein targeting |
title_sort | secyeg activates gtpases to drive the completion of cotranslational protein targeting |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575545/ https://www.ncbi.nlm.nih.gov/pubmed/23401005 http://dx.doi.org/10.1083/jcb.201208045 |
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