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Ribosome heterogeneity: another level of complexity in bacterial translation regulation
Translation of the mRNA-encoded genetic information into proteins is catalyzed by the intricate ribonucleoprotein machine, the ribosome. Historically, the bacterial ribosome is viewed as an unchangeable entity, constantly equipped with the entire complement of RNAs and proteins. Conversely, several...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Current Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3653068/ https://www.ncbi.nlm.nih.gov/pubmed/23415603 http://dx.doi.org/10.1016/j.mib.2013.01.009 |
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author | Byrgazov, Konstantin Vesper, Oliver Moll, Isabella |
author_facet | Byrgazov, Konstantin Vesper, Oliver Moll, Isabella |
author_sort | Byrgazov, Konstantin |
collection | PubMed |
description | Translation of the mRNA-encoded genetic information into proteins is catalyzed by the intricate ribonucleoprotein machine, the ribosome. Historically, the bacterial ribosome is viewed as an unchangeable entity, constantly equipped with the entire complement of RNAs and proteins. Conversely, several lines of evidence indicate the presence of functional selective ribosomal subpopulations that exhibit variations in the RNA or the protein components and modulate the translational program in response to environmental changes. Here, we summarize these findings, which raise the functional status of the ribosome from a protein synthesis machinery only to a regulatory hub that integrates environmental cues in the process of protein synthesis, thereby adding an additional level of complexity to the regulation of gene expression. |
format | Online Article Text |
id | pubmed-3653068 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Current Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-36530682013-05-14 Ribosome heterogeneity: another level of complexity in bacterial translation regulation Byrgazov, Konstantin Vesper, Oliver Moll, Isabella Curr Opin Microbiol Article Translation of the mRNA-encoded genetic information into proteins is catalyzed by the intricate ribonucleoprotein machine, the ribosome. Historically, the bacterial ribosome is viewed as an unchangeable entity, constantly equipped with the entire complement of RNAs and proteins. Conversely, several lines of evidence indicate the presence of functional selective ribosomal subpopulations that exhibit variations in the RNA or the protein components and modulate the translational program in response to environmental changes. Here, we summarize these findings, which raise the functional status of the ribosome from a protein synthesis machinery only to a regulatory hub that integrates environmental cues in the process of protein synthesis, thereby adding an additional level of complexity to the regulation of gene expression. Current Biology 2013-04 /pmc/articles/PMC3653068/ /pubmed/23415603 http://dx.doi.org/10.1016/j.mib.2013.01.009 Text en © 2013 Elsevier Ltd. https://creativecommons.org/licenses/by-nc-nd/3.0/ Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license |
spellingShingle | Article Byrgazov, Konstantin Vesper, Oliver Moll, Isabella Ribosome heterogeneity: another level of complexity in bacterial translation regulation |
title | Ribosome heterogeneity: another level of complexity in bacterial translation regulation |
title_full | Ribosome heterogeneity: another level of complexity in bacterial translation regulation |
title_fullStr | Ribosome heterogeneity: another level of complexity in bacterial translation regulation |
title_full_unstemmed | Ribosome heterogeneity: another level of complexity in bacterial translation regulation |
title_short | Ribosome heterogeneity: another level of complexity in bacterial translation regulation |
title_sort | ribosome heterogeneity: another level of complexity in bacterial translation regulation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3653068/ https://www.ncbi.nlm.nih.gov/pubmed/23415603 http://dx.doi.org/10.1016/j.mib.2013.01.009 |
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