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The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination

A new group of translation-associated heat shock genes has been recently identified. One of these novel genes is ybeY which is highly conserved in bacteria. In Escherichia coli the YbeY protein is important for efficient translation at all temperatures and is essential at high temperatures. Deletion...

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Detalles Bibliográficos
Autores principales: Grinwald, Maya, Ron, Eliora Z.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639268/
https://www.ncbi.nlm.nih.gov/pubmed/23638028
http://dx.doi.org/10.1371/journal.pone.0062297
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author Grinwald, Maya
Ron, Eliora Z.
author_facet Grinwald, Maya
Ron, Eliora Z.
author_sort Grinwald, Maya
collection PubMed
description A new group of translation-associated heat shock genes has been recently identified. One of these novel genes is ybeY which is highly conserved in bacteria. In Escherichia coli the YbeY protein is important for efficient translation at all temperatures and is essential at high temperatures. Deletion mutants of ybeY are defective in protein translation, due to impaired 30 S ribosomal subunits. Here we provide evidence which tie YbeY to the transcription antitermination process. Thus, in ybeY deletion mutants transcription is significantly inhibited when the “nut like” sequences required for transcriptional antitermination are present, while if these sequences are removed transcription is not affected by the mutation.
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spelling pubmed-36392682013-05-01 The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination Grinwald, Maya Ron, Eliora Z. PLoS One Research Article A new group of translation-associated heat shock genes has been recently identified. One of these novel genes is ybeY which is highly conserved in bacteria. In Escherichia coli the YbeY protein is important for efficient translation at all temperatures and is essential at high temperatures. Deletion mutants of ybeY are defective in protein translation, due to impaired 30 S ribosomal subunits. Here we provide evidence which tie YbeY to the transcription antitermination process. Thus, in ybeY deletion mutants transcription is significantly inhibited when the “nut like” sequences required for transcriptional antitermination are present, while if these sequences are removed transcription is not affected by the mutation. Public Library of Science 2013-04-29 /pmc/articles/PMC3639268/ /pubmed/23638028 http://dx.doi.org/10.1371/journal.pone.0062297 Text en © 2013 Grinwald, Ron http://creativecommons.org/licenses/by/4.0/ 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 author and source are properly credited.
spellingShingle Research Article
Grinwald, Maya
Ron, Eliora Z.
The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination
title The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination
title_full The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination
title_fullStr The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination
title_full_unstemmed The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination
title_short The Escherichia coli Translation-Associated Heat Shock Protein YbeY Is Involved in rRNA Transcription Antitermination
title_sort escherichia coli translation-associated heat shock protein ybey is involved in rrna transcription antitermination
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639268/
https://www.ncbi.nlm.nih.gov/pubmed/23638028
http://dx.doi.org/10.1371/journal.pone.0062297
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