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Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism
Riboswitches are noncoding mRNA elements that control gene expression by altering their structure upon metabolite binding. Although riboswitch crystal structures provide detailed information about RNA–ligand interactions, little knowledge has been gathered to understand how riboswitches modulate gen...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5602112/ https://www.ncbi.nlm.nih.gov/pubmed/28701520 http://dx.doi.org/10.1261/rna.061796.117 |
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author | Dussault, Anne-Marie Dubé, Audrey Jacques, Frédéric Grondin, Jonathan P. Lafontaine, Daniel A. |
author_facet | Dussault, Anne-Marie Dubé, Audrey Jacques, Frédéric Grondin, Jonathan P. Lafontaine, Daniel A. |
author_sort | Dussault, Anne-Marie |
collection | PubMed |
description | Riboswitches are noncoding mRNA elements that control gene expression by altering their structure upon metabolite binding. Although riboswitch crystal structures provide detailed information about RNA–ligand interactions, little knowledge has been gathered to understand how riboswitches modulate gene expression. Here, we study the molecular recognition mechanism of the S-adenosylmethionine SAM-I riboswitch by characterizing the formation of a helical stacking interaction involving the ligand-binding process. We show that ligand binding is intimately linked to the formation of the helical stacking, which is dependent on the presence of three conserved purine residues that are flanked by stacked helices. We also find that these residues are important for the formation of a crucial long-range base pair formed upon SAM binding. Together, our results lend strong support to a critical role for helical stacking in the folding pathway and suggest a particularly important function in the formation of the long-range base pair. |
format | Online Article Text |
id | pubmed-5602112 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-56021122018-10-01 Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism Dussault, Anne-Marie Dubé, Audrey Jacques, Frédéric Grondin, Jonathan P. Lafontaine, Daniel A. RNA Article Riboswitches are noncoding mRNA elements that control gene expression by altering their structure upon metabolite binding. Although riboswitch crystal structures provide detailed information about RNA–ligand interactions, little knowledge has been gathered to understand how riboswitches modulate gene expression. Here, we study the molecular recognition mechanism of the S-adenosylmethionine SAM-I riboswitch by characterizing the formation of a helical stacking interaction involving the ligand-binding process. We show that ligand binding is intimately linked to the formation of the helical stacking, which is dependent on the presence of three conserved purine residues that are flanked by stacked helices. We also find that these residues are important for the formation of a crucial long-range base pair formed upon SAM binding. Together, our results lend strong support to a critical role for helical stacking in the folding pathway and suggest a particularly important function in the formation of the long-range base pair. Cold Spring Harbor Laboratory Press 2017-10 /pmc/articles/PMC5602112/ /pubmed/28701520 http://dx.doi.org/10.1261/rna.061796.117 Text en © 2017 Dussault et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Article Dussault, Anne-Marie Dubé, Audrey Jacques, Frédéric Grondin, Jonathan P. Lafontaine, Daniel A. Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism |
title | Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism |
title_full | Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism |
title_fullStr | Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism |
title_full_unstemmed | Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism |
title_short | Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism |
title_sort | ligand recognition and helical stacking formation are intimately linked in the sam-i riboswitch regulatory mechanism |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5602112/ https://www.ncbi.nlm.nih.gov/pubmed/28701520 http://dx.doi.org/10.1261/rna.061796.117 |
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