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Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch

Significant advances in our understanding of RNA architecture, folding and recognition have emerged from structure-function studies on riboswitches, non-coding RNAs whose sensing domains bind small ligands and whose adjacent expression platforms contain RNA elements involved in the control of gene r... Full description

Journal Title: Nature 13 May 2012, Vol.486(7401), pp.85-9
Main Author: Ren, Aiming
Other Authors: Rajashankar, Kanagalaghatta R , Patel, Dinshaw J
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1476-4687 ; PMID: 22678284 Version:1 ; DOI: 10.1038/nature11152
Link: http://pubmed.gov/22678284
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recordid: medline22678284
title: Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch
format: Article
creator:
  • Ren, Aiming
  • Rajashankar, Kanagalaghatta R
  • Patel, Dinshaw J
subjects:
  • Cations, Divalent -- Chemistry
  • Fluorides -- Chemistry
  • Gram-Negative Anaerobic Straight, Curved, and Helical Rods -- Genetics
  • Magnesium -- Chemistry
  • Phosphates -- Chemistry
  • Riboswitch -- Genetics
ispartof: Nature, 13 May 2012, Vol.486(7401), pp.85-9
description: Significant advances in our understanding of RNA architecture, folding and recognition have emerged from structure-function studies on riboswitches, non-coding RNAs whose sensing domains bind small ligands and whose adjacent expression platforms contain RNA elements involved in the control of gene regulation. We now report on the ligand-bound structure of the Thermotoga petrophila fluoride riboswitch, which adopts a higher-order RNA architecture stabilized by pseudoknot and long-range reversed Watson-Crick and Hoogsteen A•U pair formation. The bound fluoride ion is encapsulated within the junctional architecture, anchored in place through direct coordination to three Mg(2+) ions, which in turn are octahedrally coordinated to water molecules and five inwardly pointing backbone phosphates. Our structure of the fluoride riboswitch in the bound state shows how RNA can form a binding pocket selective for fluoride, while discriminating against larger halide ions. The T. petrophila fluoride riboswitch probably functions in gene regulation through a transcription termination mechanism.
language: eng
source:
identifier: E-ISSN: 1476-4687 ; PMID: 22678284 Version:1 ; DOI: 10.1038/nature11152
fulltext: fulltext
issn:
  • 14764687
  • 1476-4687
url: Link


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titleFluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch
creatorRen, Aiming ; Rajashankar, Kanagalaghatta R ; Patel, Dinshaw J
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subjectCations, Divalent -- Chemistry ; Fluorides -- Chemistry ; Gram-Negative Anaerobic Straight, Curved, and Helical Rods -- Genetics ; Magnesium -- Chemistry ; Phosphates -- Chemistry ; Riboswitch -- Genetics
descriptionSignificant advances in our understanding of RNA architecture, folding and recognition have emerged from structure-function studies on riboswitches, non-coding RNAs whose sensing domains bind small ligands and whose adjacent expression platforms contain RNA elements involved in the control of gene regulation. We now report on the ligand-bound structure of the Thermotoga petrophila fluoride riboswitch, which adopts a higher-order RNA architecture stabilized by pseudoknot and long-range reversed Watson-Crick and Hoogsteen A•U pair formation. The bound fluoride ion is encapsulated within the junctional architecture, anchored in place through direct coordination to three Mg(2+) ions, which in turn are octahedrally coordinated to water molecules and five inwardly pointing backbone phosphates. Our structure of the fluoride riboswitch in the bound state shows how RNA can form a binding pocket selective for fluoride, while discriminating against larger halide ions. The T. petrophila fluoride riboswitch probably functions in gene regulation through a transcription termination mechanism.
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descriptionSignificant advances in our understanding of RNA architecture, folding and recognition have emerged from structure-function studies on riboswitches, non-coding RNAs whose sensing domains bind small ligands and whose adjacent expression platforms contain RNA elements involved in the control of gene regulation. We now report on the ligand-bound structure of the Thermotoga petrophila fluoride riboswitch, which adopts a higher-order RNA architecture stabilized by pseudoknot and long-range reversed Watson-Crick and Hoogsteen A•U pair formation. The bound fluoride ion is encapsulated within the junctional architecture, anchored in place through direct coordination to three Mg(2+) ions, which in turn are octahedrally coordinated to water molecules and five inwardly pointing backbone phosphates. Our structure of the fluoride riboswitch in the bound state shows how RNA can form a binding pocket selective for fluoride, while discriminating against larger halide ions. The T. petrophila fluoride riboswitch probably functions in gene regulation through a transcription termination mechanism.
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abstractSignificant advances in our understanding of RNA architecture, folding and recognition have emerged from structure-function studies on riboswitches, non-coding RNAs whose sensing domains bind small ligands and whose adjacent expression platforms contain RNA elements involved in the control of gene regulation. We now report on the ligand-bound structure of the Thermotoga petrophila fluoride riboswitch, which adopts a higher-order RNA architecture stabilized by pseudoknot and long-range reversed Watson-Crick and Hoogsteen A•U pair formation. The bound fluoride ion is encapsulated within the junctional architecture, anchored in place through direct coordination to three Mg(2+) ions, which in turn are octahedrally coordinated to water molecules and five inwardly pointing backbone phosphates. Our structure of the fluoride riboswitch in the bound state shows how RNA can form a binding pocket selective for fluoride, while discriminating against larger halide ions. The T. petrophila fluoride riboswitch probably functions in gene regulation through a transcription termination mechanism.
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