Abstract
Riboswitches are widely found in the 5'-UTR of bacterial mRNA. They function as cis-acting regulatory elements and control protein expression through binding ligands. Ligand recognition and specificity have been well studied by structural determination of ligand-bound states. However, ligand-free conformations and conformational interconversions remain poorly understood, yet they are essential for riboswitch functions. Here we analyzed both ligand-bound and ligand-free conformations of the SAM/SAH riboswitch and determined the folding energy landscape of this translational riboswitch using single-molecule FRET, and related this to our crystal structure of the ligand-bound riboswitch.
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