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tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation
Since accurate translation from mRNA to protein is critical to survival, cells have developed translational quality control systems. Bacterial ribosomes stalled on truncated mRNA are rescued by a system involving tmRNA and SmpB referred to as trans-translation. Here, we review current understanding...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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SAGE-Hindawi Access to Research
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022190/ https://www.ncbi.nlm.nih.gov/pubmed/21253384 http://dx.doi.org/10.4061/2011/130581 |
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author | Kurita, Daisuke Muto, Akira Himeno, Hyouta |
author_facet | Kurita, Daisuke Muto, Akira Himeno, Hyouta |
author_sort | Kurita, Daisuke |
collection | PubMed |
description | Since accurate translation from mRNA to protein is critical to survival, cells have developed translational quality control systems. Bacterial ribosomes stalled on truncated mRNA are rescued by a system involving tmRNA and SmpB referred to as trans-translation. Here, we review current understanding of the mechanism of trans-translation. Based on results obtained by using directed hydroxyl radical probing, we propose a new type of molecular mimicry during trans-translation. Besides such chemical approaches, biochemical and cryo-EM studies have revealed the structural and functional aspects of multiple stages of trans-translation. These intensive works provide a basis for studying the dynamics of tmRNA/SmpB in the ribosome. |
format | Text |
id | pubmed-3022190 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | SAGE-Hindawi Access to Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-30221902011-01-20 tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation Kurita, Daisuke Muto, Akira Himeno, Hyouta J Nucleic Acids Review Article Since accurate translation from mRNA to protein is critical to survival, cells have developed translational quality control systems. Bacterial ribosomes stalled on truncated mRNA are rescued by a system involving tmRNA and SmpB referred to as trans-translation. Here, we review current understanding of the mechanism of trans-translation. Based on results obtained by using directed hydroxyl radical probing, we propose a new type of molecular mimicry during trans-translation. Besides such chemical approaches, biochemical and cryo-EM studies have revealed the structural and functional aspects of multiple stages of trans-translation. These intensive works provide a basis for studying the dynamics of tmRNA/SmpB in the ribosome. SAGE-Hindawi Access to Research 2011-01-05 /pmc/articles/PMC3022190/ /pubmed/21253384 http://dx.doi.org/10.4061/2011/130581 Text en Copyright © 2011 Daisuke Kurita et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Kurita, Daisuke Muto, Akira Himeno, Hyouta tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation |
title | tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation |
title_full | tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation |
title_fullStr | tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation |
title_full_unstemmed | tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation |
title_short | tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation |
title_sort | trna/mrna mimicry by tmrna and smpb in trans-translation |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022190/ https://www.ncbi.nlm.nih.gov/pubmed/21253384 http://dx.doi.org/10.4061/2011/130581 |
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