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- W2019445565 abstract "Riboswitches, found in the 5′ untranslated regions of bacterial messenger RNA (mRNA), regulate gene expression through secondary or tertiary structural changes induced by metabolite binding. Localized conformational changes near the metabolite-binding site alter downstream secondary structure, ultimately determining gene expression. This ribo-regulation of gene expression depends significantly on the kinetics and thermodynamics of the structural changes of the mRNA and metabolite binding, and therefore a thorough understanding of these dynamics is crucial to developing a complete knowledge of the riboswitch functionality. In an effort to probe the folding interactions of riboswitches, the 208-nucleotide metabolite-binding domain of the Bacillus subtilis lysine riboswitch was prepared by transcription and hybridization to a dual fluorescent label RNA strand, which allowed FRET monitoring of structural changes. Ensemble measurements revealed structural sensitivity to monovalent (Na+, K+) and divalent (Mg2+) cations. The RNA construct was also studied using time-resolved-single-molecule FRET (smFRET) methods that allow for thorough characterization of the riboswitch-folding dynamics under equilibrium conditions. The effects of cations on the tertiary folding/unfolding of the lysine riboswitch were investigated. Single-molecule studies were performed on freely diffusing riboswitches, as well as, riboswitches tethered to surfaces. The freely diffusing studies allow one to investigate and resolve conformational populations in solution, while the surface tethered experiments allow one to resolve the individual folding and unfolding rate constants." @default.
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- W2019445565 date "2009-02-01" @default.
- W2019445565 modified "2023-09-28" @default.
- W2019445565 title "Single-Molecule FRET Studies of Lysine Riboswitch Folding" @default.
- W2019445565 doi "https://doi.org/10.1016/j.bpj.2008.12.3010" @default.
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