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Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB
Ribosome stalling is a serious issue for cell survival. In bacteria, the primary rescue system is trans-translation, performed by tmRNA and its protein partner small protein B (SmpB). Since its discovery almost 20 years ago, biochemical, genetic, and structural studies have paved the way to a better...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3968760/ https://www.ncbi.nlm.nih.gov/pubmed/24711807 http://dx.doi.org/10.3389/fmicb.2014.00113 |
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author | Giudice, Emmanuel Macé, Kevin Gillet, Reynald |
author_facet | Giudice, Emmanuel Macé, Kevin Gillet, Reynald |
author_sort | Giudice, Emmanuel |
collection | PubMed |
description | Ribosome stalling is a serious issue for cell survival. In bacteria, the primary rescue system is trans-translation, performed by tmRNA and its protein partner small protein B (SmpB). Since its discovery almost 20 years ago, biochemical, genetic, and structural studies have paved the way to a better understanding of how this sophisticated process takes place at the cellular and molecular levels. Here we describe the molecular details of trans-translation, with special mention of recent cryo-electron microscopy and crystal structures that have helped explain how the huge tmRNA-SmpB complex targets and delivers stalled ribosomes without interfering with canonical translation. |
format | Online Article Text |
id | pubmed-3968760 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-39687602014-04-07 Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB Giudice, Emmanuel Macé, Kevin Gillet, Reynald Front Microbiol Microbiology Ribosome stalling is a serious issue for cell survival. In bacteria, the primary rescue system is trans-translation, performed by tmRNA and its protein partner small protein B (SmpB). Since its discovery almost 20 years ago, biochemical, genetic, and structural studies have paved the way to a better understanding of how this sophisticated process takes place at the cellular and molecular levels. Here we describe the molecular details of trans-translation, with special mention of recent cryo-electron microscopy and crystal structures that have helped explain how the huge tmRNA-SmpB complex targets and delivers stalled ribosomes without interfering with canonical translation. Frontiers Media S.A. 2014-03-21 /pmc/articles/PMC3968760/ /pubmed/24711807 http://dx.doi.org/10.3389/fmicb.2014.00113 Text en Copyright © 2014 Giudice, Macé and Gillet. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Giudice, Emmanuel Macé, Kevin Gillet, Reynald Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB |
title | Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB |
title_full | Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB |
title_fullStr | Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB |
title_full_unstemmed | Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB |
title_short | Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB |
title_sort | trans-translation exposed: understanding the structures and functions of tmrna-smpb |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3968760/ https://www.ncbi.nlm.nih.gov/pubmed/24711807 http://dx.doi.org/10.3389/fmicb.2014.00113 |
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