Metabolite recognition principles and molecular mechanisms underlying riboswitch function Journal Article


Authors: Serganov, A.; Patel, D. J.
Article Title: Metabolite recognition principles and molecular mechanisms underlying riboswitch function
Abstract: Riboswitches are mRNA elements capable of modulating gene expression in response to specific binding by cellular metabolites. Riboswitches exert their function through the interplay of alternative ligand-free and ligand-bound conformations of the metabolite-sensing domain, which in turn modulate the formation of adjacent gene expression controlling elements. X-ray crystallography and NMR spectroscopy have determined three-dimensional structures of virtually all the major riboswitch classes in the ligand-bound state and, for several riboswitches, in the ligand-free state. The resulting spatial topologies have demonstrated the wide diversity of riboswitch folds and revealed structural principles for specific recognition by cognate metabolites. The available three-dimensional information, supplemented by structure-guided biophysical and biochemical experimentation, has led to an improved understanding of how riboswitches fold, what RNA conformations are required for ligand recognition, and how ligand binding can be transduced into gene expression modulation. These studies have greatly facilitated the dissection of molecular mechanisms underlying riboswitch action and should in turn guide the anticipated development of tools for manipulating gene regulatory circuits. © 2012 by Annual Reviews. All rights reserved.
Keywords: x-ray crystallography; nmr; ligand-binding pockets; metal ions; rna structure and folding
Journal Title: Annual Review of Biophysics
Volume: 41
Issue: 1
ISSN: 1936-122X
Publisher: Annual Reviews  
Date Published: 2012-06-09
Start Page: 343
End Page: 370
Language: English
DOI: 10.1146/annurev-biophys-101211-113224
PROVIDER: scopus
PUBMED: 22577823
PMCID: PMC4696762
DOI/URL:
Notes: --- - "Export Date: 4 June 2012" - "Source: Scopus"
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  1. Dinshaw J Patel
    479 Patel