ArticleJournal of molecular biology2007
Group II intron folding under near-physiological conditions: collapsing to the near-native state.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 53 citations in OpenAlex.
- Dynamic assembly of a large multidomain ribozyme visualized by cryo-electron microscopy.Nature communications · 2025Article
- LncRNA SChLAP1 Promotes Cancer Cell Proliferation and Invasion Via Its Distinct Structural Domains and Conserved Regions.Journal of molecular biology · 2025Article
- Computational De Novo Design of Group II Introns Yields Highly Active Ribozymes.Chembiochem : a European journal of chemical biology · 2025Article
- Effects of Preferential Counterion Interactions on the Specificity of RNA Folding.The journal of physical chemistry letters · 2018Article
- Assembly and dynamics of the U4/U6 di-snRNP by single-molecule FRET.Nucleic acids research · 2015Article
- How do metal ions direct ribozyme folding?Nature chemistry · 2015Article
- Native Purification and Analysis of Long RNAs.Methods in enzymology · 2015Article
- Mss116p: a DEAD-box protein facilitates RNA folding.RNA biology · 2013Review
- The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate.Journal of molecular biology · 2012Article
- RNA catalysis as a probe for chaperone activity of DEAD-box helicases.Methods in enzymology · 2012Article
- ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo.Journal of molecular biology · 2011Article
- Article
- Dual roles for the Mss116 cofactor during splicing of the ai5γ group II intron.Nucleic acids research · 2010Article
- The tertiary structure of group II introns: implications for biological function and evolution.Critical reviews in biochemistry and molecular biology · 2010Review
- Protein-facilitated folding of group II intron ribozymes.Journal of molecular biology · 2010Article
- Compact intermediates in RNA folding.Annual review of biophysics · 2010Review
- Single-molecule studies of group II intron ribozymes.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A conserved element that stabilizes the group II intron active site.RNA (New York, N.Y.) · 2008Article
- A kinetic intermediate that regulates proper folding of a group II intron RNA.Journal of molecular biology · 2008Article
- Do DEAD-box proteins promote group II intron splicing without unwinding RNA?Molecular cell · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The folding of group II intron ribozymes has been studied extensively under optimal conditions for self-splicing in vitro (42 degrees C and high magnesium ion concentrations). In these cases, the ribozymes fold directly to the native state by an apparent two-state mechanism involving the formation of an obligate intermediate within intron domain 1. We have now characterized the folding pathway under near-physiological conditions. We observe that compaction of the RNA proceeds slowly to completion, even at low magnesium concentration (3 mM). Kinetic analysis shows that this compact species is a "near-native" intermediate state that is readily chased into the native state by the addition of high salt. Structural probing reveals that the near-native state represents a compact domain 1 scaffold that is not yet docked with the catalytic domains (D3 and D5). Interestingly, native ribozyme reverts to the near-native state upon reduction in magnesium concentration. Therefore, while the intron can sustain the intermediate state under physiological conditions, the native structure is not maintained and is likely to require stabilization by protein cofactors in vivo.
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