ArticleRNA (New York, N.Y.)2006
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme.
Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Pushing the Limits of Nucleic Acid Function.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Review
- Bacterial group I introns: mobile RNA catalysts.Mobile DNA · 2014Article
- Synthetic shuffling and in vitro selection reveal the rugged adaptive fitness landscape of a kinase ribozyme.RNA (New York, N.Y.) · 2013Article
- Evolutionary evidence for alternative structure in RNA sequence co-variation.PLoS computational biology · 2013Article
- Enhanced specificity against misfolding in a thermostable mutant of the Tetrahymena ribozyme.Biochemistry · 2011Article
- Crystal structure of the lysine riboswitch regulatory mRNA element.The Journal of biological chemistry · 2008Article
- High-throughput single-nucleotide structural mapping by capillary automated footprinting analysis.Nucleic acids research · 2008Article
- Tertiary interactions determine the accuracy of RNA folding.Journal of the American Chemical Society · 2008Article
- Local RNA structural changes induced by crystallization are revealed by SHAPE.RNA (New York, N.Y.) · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although general mechanisms of RNA folding and catalysis have been elucidated, little is known about how ribozymes achieve structural stability at high temperature. A previous in vitro evolution experiment identified a small number of mutations that significantly increase the thermostability of the tertiary structure of the Tetrahymena ribozyme. Because we also determined the crystal structure of this thermostable ribozyme, we have for the first time the opportunity to compare the structural interactions and thermodynamic contributions of individual nucleotides in a ribozyme. We investigated the contribution of five mutations to thermostability by using temperature gradient gel electrophoresis. Unlike the case with several well-studied proteins, the effects of individual mutations on thermostability of this RNA were highly context dependent. The three most important mutations for thermostability were actually destabilizing in the wild-type background. A269G and A304G contributed to stability only when present as a pair, consistent with their proximity in the ribozyme structure. In an evolutionary context, this work supports and extends the idea that one advantage of protein enzyme systems over an RNA world is the ability of proteins to accumulate stabilizing single-site mutations, whereas RNA may often require much rarer double mutations to improve the stability of both its tertiary and secondary structures.
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