ArticleThe Journal of biological chemistry2011
The Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 33 citations in OpenAlex.
- RNA functional modulation by Mitoxantrone via RNA structural ensemble repartitioning.Nature communications · 2026Article
- Universal cold RNA phase transitions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Watching ion-driven kinetics of ribozyme folding and misfolding caused by energetic and topological frustration one molecule at a time.Nucleic acids research · 2023Article
- Topological crossing in the misfoldedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Dynamic RNA Fitness Landscapes of a Group I Ribozyme during Changes to the Experimental Environment.Molecular biology and evolution · 2022Article
- Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Negative Epistasis in Experimental RNA Fitness Landscapes.Journal of molecular evolution · 2017Review
- Comparative Visualization of the RNA Suboptimal Conformational Ensemble In Vivo.Biophysical journal · 2017Article
- Nucleobases Undergo Dynamic Rearrangements during RNA Tertiary Folding.Journal of molecular biology · 2016Article
- Secondary structure encodes a cooperative tertiary folding funnel in the Azoarcus ribozyme.Nucleic acids research · 2016Article
- Formation of Tertiary Interactions during rRNA GTPase Center Folding.Journal of molecular biology · 2015Article
- Detecting riboSNitches with RNA folding algorithms: a genome-wide benchmark.Nucleic acids research · 2015Article
- Molecular crowding overcomes the destabilizing effects of mutations in a bacterial ribozyme.Nucleic acids research · 2015Article
- A kinetic and thermodynamic framework for the Azoarcus group I ribozyme reaction.RNA (New York, N.Y.) · 2014Article
- Article
- Folding pathways of the Tetrahymena ribozyme.Journal of molecular biology · 2014Article
- Structural dynamics of a mitochondrial tRNA possessing weak thermodynamic stability.Biochemistry · 2014Article
- Bacterial group I introns: mobile RNA catalysts.Mobile DNA · 2014Article
- Trans-splicing with the group I intron ribozyme from Azoarcus.RNA (New York, N.Y.) · 2014Article
- Increased ribozyme activity in crowded solutions.The Journal of biological chemistry · 2014Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Structured RNAs traverse complex energy landscapes that include valleys representing misfolded intermediates. In Neurospora crassa and Saccharomyces cerevisiae, efficient splicing of mitochondrial group I and II introns requires the DEAD box proteins CYT-19 and Mss116p, respectively, which promote folding transitions and function as general RNA chaperones. To test the generality of RNA misfolding and the activities of DEAD box proteins in vitro, here we measure native folding of a small group I intron ribozyme from the bacterium Azoarcus by monitoring its catalytic activity. To develop this assay, we first measure cleavage of an oligonucleotide substrate by the prefolded ribozyme. Substrate cleavage is rate-limited by binding and is readily reversible, with an internal equilibrium near unity, such that the amount of product observed is less than the amount of native ribozyme. We use this assay to show that approximately half of the ribozyme folds readily to the native state, whereas the other half forms an intermediate that transitions slowly to the native state. This folding transition is accelerated by urea and increased temperature and slowed by increased Mg(2+) concentration, suggesting that the intermediate is misfolded and must undergo transient unfolding during refolding to the native state. CYT-19 and Mss116p accelerate refolding in an ATP-dependent manner, presumably by disrupting structure in the intermediate. These results highlight the tendency of RNAs to misfold, underscore the roles of CYT-19 and Mss116p as general RNA chaperones, and identify a refolding transition for further dissection of the roles of DEAD box proteins in RNA folding.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.