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Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch
The ever-changing environment of a bacterial cell requires sophisticated mechanisms to adjust gene expression in response to changes in nutrient availability. L box riboswitch RNAs regulate gene expression in response to cellular lysine (lys) concentrations in the absence of additional regulatory fa...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384330/ https://www.ncbi.nlm.nih.gov/pubmed/22416067 http://dx.doi.org/10.1093/nar/gks212 |
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author | Wilson-Mitchell, Sharnise N. Grundy, Frank J. Henkin, Tina M. |
author_facet | Wilson-Mitchell, Sharnise N. Grundy, Frank J. Henkin, Tina M. |
author_sort | Wilson-Mitchell, Sharnise N. |
collection | PubMed |
description | The ever-changing environment of a bacterial cell requires sophisticated mechanisms to adjust gene expression in response to changes in nutrient availability. L box riboswitch RNAs regulate gene expression in response to cellular lysine (lys) concentrations in the absence of additional regulatory factors. In Bacillus subtilis, binding of lysine (lys) to the L box RNA causes premature transcription termination in the leader region upstream of the lysC coding sequence. To date, little is known about the specific RNA–lys interactions required for transcription termination. In this study, we characterize features of the B. subtilis lysC leader RNA responsible for lys specificity, and structural elements of the lys molecule required for recognition. The wild-type lysC leader RNA can recognize and discriminate between lys and lys analogs. We identified leader RNA variants with mutations in the lys-binding pocket that exhibit changes in the specificity of ligand recognition. These data demonstrate that lysC leader RNA specificity is the result of recognition of ligand features through a series of distinct interactions between lys and nucleotides that comprise the lys-binding pocket, and provide insight into the molecular mechanisms employed by L box riboswitch RNAs to bind and recognize lys. |
format | Online Article Text |
id | pubmed-3384330 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-33843302012-06-28 Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch Wilson-Mitchell, Sharnise N. Grundy, Frank J. Henkin, Tina M. Nucleic Acids Res RNA The ever-changing environment of a bacterial cell requires sophisticated mechanisms to adjust gene expression in response to changes in nutrient availability. L box riboswitch RNAs regulate gene expression in response to cellular lysine (lys) concentrations in the absence of additional regulatory factors. In Bacillus subtilis, binding of lysine (lys) to the L box RNA causes premature transcription termination in the leader region upstream of the lysC coding sequence. To date, little is known about the specific RNA–lys interactions required for transcription termination. In this study, we characterize features of the B. subtilis lysC leader RNA responsible for lys specificity, and structural elements of the lys molecule required for recognition. The wild-type lysC leader RNA can recognize and discriminate between lys and lys analogs. We identified leader RNA variants with mutations in the lys-binding pocket that exhibit changes in the specificity of ligand recognition. These data demonstrate that lysC leader RNA specificity is the result of recognition of ligand features through a series of distinct interactions between lys and nucleotides that comprise the lys-binding pocket, and provide insight into the molecular mechanisms employed by L box riboswitch RNAs to bind and recognize lys. Oxford University Press 2012-07 2012-03-13 /pmc/articles/PMC3384330/ /pubmed/22416067 http://dx.doi.org/10.1093/nar/gks212 Text en © The Author(s) 2012. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | RNA Wilson-Mitchell, Sharnise N. Grundy, Frank J. Henkin, Tina M. Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch |
title | Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch |
title_full | Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch |
title_fullStr | Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch |
title_full_unstemmed | Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch |
title_short | Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch |
title_sort | analysis of lysine recognition and specificity of the bacillus subtilis l box riboswitch |
topic | RNA |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384330/ https://www.ncbi.nlm.nih.gov/pubmed/22416067 http://dx.doi.org/10.1093/nar/gks212 |
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