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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...

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Detalles Bibliográficos
Autores principales: Kurita, Daisuke, Muto, Akira, Himeno, Hyouta
Formato: Texto
Lenguaje:English
Publicado: SAGE-Hindawi Access to Research 2011
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.
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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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