Single-molecule studies of the lysine riboswitch reveal effector-dependent conformational dynamics of the aptamer domain.

ABSTRACT: The lysine riboswitch is a cis-acting RNA genetic regulatory element found in the leader sequence of bacterial mRNAs coding for proteins related to biosynthesis or transport of lysine. Structural analysis of the lysine-binding aptamer domain of this RNA has revealed that it completely encapsulates the ligand and therefore must undergo a structural opening/closing upon interaction with lysine. In this work, single-molecule fluorescence resonance energy transfer (FRET) methods are used to monitor these ligand-induced structural transitions that are central to lysine riboswitch function. Specifically, a model FRET system has been developed for characterizing the lysine dissociation constant as well as the opening/closing rate constants for the Bacillus subtilis lysC aptamer domain. These tech

SUBMITTER: Fiegland LR 

PROVIDER: S-EPMC3703957 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature