Thermodynamics and Kinetics of Adaptive Binding in the Malachite Green RNA Aptamer
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Date
2013-09-24
Authors
Da Costa, Jason B.
Andreiev, Aurelia I.
Dieckmann, Thorsten
Journal Title
Journal ISSN
Volume Title
Publisher
American Chemical Society
Abstract
Adaptive binding, the ability of molecules to fold themselves around the structure of a ligand and thereby incorporating it into their three-dimensional fold, is a key feature of most RNA aptamers. The malachite green aptamer (MGA) has been shown to bind several closely related triphenyl dyes with planar and nonplanar structures in this manner. Competitive binding studies using isothermal titration calorimetry and stopped flow kinetics have been conducted with the aim of understanding the adaptive nature of RNA–ligand interaction. The results of these studies reveal that binding of one ligand can reduce the ability of the aptamer pocket to adapt to another ligand, even if this second ligand has a significantly higher affinity to the free aptamer. A similar effect is observed in the presence of Mg2+ ions which stabilize the binding pocket in a more ligand bound-like conformation.
Description
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright © American Chemical Society after peer review and technical editing by publisher. To access the final edited and published work see http://dx.doi.org/10.1021/bi400549s
Keywords
Isothermal Titration Calorimetry, Ligand-Binding, Cross-Relaxation, Riboswitch, Recognition, Fluorescence, Spectroscopy, Suppression, Polymerase, Networks