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Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Investigating the ion dependence of the first unfolding step of GTPase-Associating Center ribosomal RNA.
Journal of Biomolecular Structure & Dynamics 2018 January
The interactions in the tertiary structure of a ribosomal RNA fragment in the GTPase Associating Center (GAC) have been experimentally studied, but the roles of the bound and diffuse cations in its folding pathway have not yet been fully elucidated. Melting experiments have shown that the temperature of the first of the two distinguishable transitions in the unfolding pathway of the GAC RNA can be regulated by altering the magnesium concentration, yet the physical interpretation of such ion-dependent effects on folding have not been clearly understood in spite of the availability of crystal structures that depict many GAC RNA-ion interactions. Here, we use umbrella sampling and molecular dynamics (MD) simulations to provide a physical description for the first transition in this unfolding pathway, with a focus on the role of a chelated magnesium ion. Our results indicate that the presence of cations mediating the local interaction of two loops stabilizes the folded state relative to the unfolded or partially folded states. Also, our findings suggest that a bridging magnesium ion between the two loops improves the stabilizing effect. This is consistent with the multistep unfolding pathway proposed for the GAC RNA and highlights the importance of ions in the first unfolding step. The results suggest how MD simulations can provide insight into RNA unfolding pathways as a complementary approach to experiments.
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