Abstract

In Saccharomyces cerevisiae, ribosomal protein L30e acts as an autoregulator by inhibiting the splicing and translation of its mRNA. The L30 protein-RNA binding site has been previously studied, revealing a kink-turn motif, which is characterized by a sharp bend in the phosphodiester backbone due to unpaired nucleotides and internal tertiary interactions. The 3D structure of the kink-turn is critical for L30e binding. Preliminary studies utilizing analytical ultracentrifugation (AUC) reveal that kink-turned RNA is more sharply bent in the presence of magnesium (Mg2+) than in its absence; no structural change was observed upon addition of Mg2+ when the kink-turn was disrupted. This confirms the hypothesis that, in solution, the kink-turn exists in equilibrium between a more open and tightly bent conformation, and that addition of Mg2+ shifts this toward the sharply kinked structure.

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