Single molecule ligand binding kinetics and environmental adaptations in lysine riboswitches
Abstract: Riboswitches are important RNA structures in bacteria and some eukaryotes that can bind a ligand to toggle between conformations that allow or terminate transcription, translation, or splicing. We study folding kinetics and thermodynamics in the B. subtilis and T. maritima lysine riboswitches via single molecule TIRF microscopy. We show that riboswitch folding is exothermic with a large entropic cost, which we attribute to increased binding pocket rigidity upon lysine binding.