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Quality Control Mechanisms in Bacterial Translation
Ribosome stalling during translation significantly reduces cell viability, because cells have to spend resources on the synthesis of new ribosomes. Therefore, all bacteria have developed various mechanisms of ribosome rescue. Usually, the release of ribosomes is preceded by hydrolysis of the tRNA–pe...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
A.I. Gordeyev
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8327144/ https://www.ncbi.nlm.nih.gov/pubmed/34377554 http://dx.doi.org/10.32607/actanaturae.11401 |
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author | Zarechenskaia, A. S. Sergiev, P. V. Osterman, I. A. |
author_facet | Zarechenskaia, A. S. Sergiev, P. V. Osterman, I. A. |
author_sort | Zarechenskaia, A. S. |
collection | PubMed |
description | Ribosome stalling during translation significantly reduces cell viability, because cells have to spend resources on the synthesis of new ribosomes. Therefore, all bacteria have developed various mechanisms of ribosome rescue. Usually, the release of ribosomes is preceded by hydrolysis of the tRNA–peptide bond, but, in some cases, the ribosome can continue translation thanks to the activity of certain factors. This review describes the mechanisms of ribosome rescue thanks to trans-translation and the activity of the ArfA, ArfB, BrfA, ArfT, HflX, and RqcP/H factors, as well as continuation of translation via the action of EF-P, EF-4, and EttA. Despite the ability of some systems to duplicate each other, most of them have their unique functional role, related to the quality control of bacterial translation in certain abnormalities caused by mutations, stress cultivation conditions, or antibiotics. |
format | Online Article Text |
id | pubmed-8327144 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | A.I. Gordeyev |
record_format | MEDLINE/PubMed |
spelling | pubmed-83271442021-08-09 Quality Control Mechanisms in Bacterial Translation Zarechenskaia, A. S. Sergiev, P. V. Osterman, I. A. Acta Naturae Research Article Ribosome stalling during translation significantly reduces cell viability, because cells have to spend resources on the synthesis of new ribosomes. Therefore, all bacteria have developed various mechanisms of ribosome rescue. Usually, the release of ribosomes is preceded by hydrolysis of the tRNA–peptide bond, but, in some cases, the ribosome can continue translation thanks to the activity of certain factors. This review describes the mechanisms of ribosome rescue thanks to trans-translation and the activity of the ArfA, ArfB, BrfA, ArfT, HflX, and RqcP/H factors, as well as continuation of translation via the action of EF-P, EF-4, and EttA. Despite the ability of some systems to duplicate each other, most of them have their unique functional role, related to the quality control of bacterial translation in certain abnormalities caused by mutations, stress cultivation conditions, or antibiotics. A.I. Gordeyev 2021 /pmc/articles/PMC8327144/ /pubmed/34377554 http://dx.doi.org/10.32607/actanaturae.11401 Text en Copyright ® 2021 National Research University Higher School of Economics. https://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Zarechenskaia, A. S. Sergiev, P. V. Osterman, I. A. Quality Control Mechanisms in Bacterial Translation |
title | Quality Control Mechanisms in Bacterial Translation |
title_full | Quality Control Mechanisms in Bacterial Translation |
title_fullStr | Quality Control Mechanisms in Bacterial Translation |
title_full_unstemmed | Quality Control Mechanisms in Bacterial Translation |
title_short | Quality Control Mechanisms in Bacterial Translation |
title_sort | quality control mechanisms in bacterial translation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8327144/ https://www.ncbi.nlm.nih.gov/pubmed/34377554 http://dx.doi.org/10.32607/actanaturae.11401 |
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