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The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1

Internal ribosome entry sites (IRESs) are RNA elements capable of initiating translation on an internal portion of a messenger RNA. The intergenic region (IGR) IRES of the Dicistroviridae virus family folds into a triple pseudoknot tertiary structure, allowing it to recruit the ribosome and initiate...

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Autores principales: Roberts, Luc, Wieden, Hans-Joachim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9458429/
https://www.ncbi.nlm.nih.gov/pubmed/36039756
http://dx.doi.org/10.1093/nar/gkac697
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author Roberts, Luc
Wieden, Hans-Joachim
author_facet Roberts, Luc
Wieden, Hans-Joachim
author_sort Roberts, Luc
collection PubMed
description Internal ribosome entry sites (IRESs) are RNA elements capable of initiating translation on an internal portion of a messenger RNA. The intergenic region (IGR) IRES of the Dicistroviridae virus family folds into a triple pseudoknot tertiary structure, allowing it to recruit the ribosome and initiate translation in a structure dependent manner. This IRES has also been reported to drive translation in Escherichia coli and to date is the only described translation initiation signal that functions across domains of life. Here we show that unlike in the eukaryotic context the tertiary structure of the IGR IRES is not required for prokaryotic ribosome recruitment. In E. coli IGR IRES translation efficiency is dependent on ribosomal protein S1 in conjunction with an AG-rich Shine-Dalgarno-like element, supporting a model where the translational activity of the IGR IRESs is due to S1-mediated canonical prokaryotic translation.
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spelling pubmed-94584292022-09-09 The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1 Roberts, Luc Wieden, Hans-Joachim Nucleic Acids Res RNA and RNA-protein complexes Internal ribosome entry sites (IRESs) are RNA elements capable of initiating translation on an internal portion of a messenger RNA. The intergenic region (IGR) IRES of the Dicistroviridae virus family folds into a triple pseudoknot tertiary structure, allowing it to recruit the ribosome and initiate translation in a structure dependent manner. This IRES has also been reported to drive translation in Escherichia coli and to date is the only described translation initiation signal that functions across domains of life. Here we show that unlike in the eukaryotic context the tertiary structure of the IGR IRES is not required for prokaryotic ribosome recruitment. In E. coli IGR IRES translation efficiency is dependent on ribosomal protein S1 in conjunction with an AG-rich Shine-Dalgarno-like element, supporting a model where the translational activity of the IGR IRESs is due to S1-mediated canonical prokaryotic translation. Oxford University Press 2022-08-30 /pmc/articles/PMC9458429/ /pubmed/36039756 http://dx.doi.org/10.1093/nar/gkac697 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle RNA and RNA-protein complexes
Roberts, Luc
Wieden, Hans-Joachim
The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1
title The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1
title_full The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1
title_fullStr The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1
title_full_unstemmed The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1
title_short The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1
title_sort prokaryotic activity of the igr iress is mediated by ribosomal protein s1
topic RNA and RNA-protein complexes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9458429/
https://www.ncbi.nlm.nih.gov/pubmed/36039756
http://dx.doi.org/10.1093/nar/gkac697
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