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• W1968086656 abstract "The catalysis of site-specific RNA cleavage and ligation by the hairpin ribozyme requires the formation of a tertiary interaction between two independently folded internal loop domains, A and B. Within the B domain, a tertiary structure has been identified, known as the loop E motif, that has been observed in many naturally occurring RNAs. One characteristic of this motif is a partial cross-strand stack of a G residue on a U residue. In a few cases, including loop B of the hairpin ribozyme, this unusual arrangement gives rise to photoreactivity. In the hairpin, G21 and U42 can be UV cross-linked. Here we show that docking of the two domains correlates very strongly with a loss of UV reactivity of these bases. The rate of the loss of photoreactivity during folding is in close agreement with the kinetics of interdomain docking as determined by hydroxyl-radical footprinting and fluorescence resonance energy transfer (FRET). Fixing the structure of the complex in the cross-linked form results in an inability of the two domains to dock and catalyze the cleavage reaction, suggesting that the conformational change is essential for catalysis." @default.
• W1968086656 created "2016-06-24" @default.
• W1968086656 creator A5002748007 @default.
• W1968086656 creator A5058839290 @default.
• W1968086656 date "2001-03-01" @default.
• W1968086656 modified "2023-10-07" @default.
• W1968086656 title "A Conformational Change in the “Loop E-like” Motif of the Hairpin Ribozyme Is Coincidental with Domain Docking and Is Essential for Catalysis" @default.
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• W1968086656 doi "https://doi.org/10.1021/bi0028385" @default.
• W1968086656 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11297441" @default.
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