ArticleGenes & development2002
RNA chaperone StpA loosens interactions of the tertiary structure in the td group I intron in vivo.
Article in Genes & development, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
46 citing papers in PubMed, 86 citations in OpenAlex.
- Selective targeting of a histone-like silencer Sfx to the R6K conjugal transfer operon.bioRxiv : the preprint server for biology · 2026Article
- A high-throughput search for intracellular factors that affect RNA folding identifiesRNA biology · 2024Article
- The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements.Nucleic acids research · 2021Article
- αβDCA method identifies unspecific binding but specific disruption of the group I intron by the StpA chaperone.RNA (New York, N.Y.) · 2020Article
- The Sac10b homolog from Sulfolobus islandicus is an RNA chaperone.Nucleic acids research · 2020Article
- Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.Signal transduction and targeted therapy · 2020Review
- Histone-like Nucleoid-Structuring Protein (H-NS) Paralogue StpA Activates the Type I-E CRISPR-Cas System against Natural Transformation in Escherichia coli.Applied and environmental microbiology · 2020Article
- Advances in RNA 3D Structure Modeling Using Experimental Data.Frontiers in genetics · 2020Review
- The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets.Nucleic acids research · 2017Article
- Probing the structure of ribosome assembly intermediates in vivo using DMS and hydroxyl radical footprinting.Methods (San Diego, Calif.) · 2016Article
- Progress and challenges for chemical probing of RNA structure inside living cells.Nature chemical biology · 2015Review
- Exploiting post-transcriptional regulation to probe RNA structures in vivo via fluorescence.Nucleic acids research · 2015Article
- 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
- On the importance of cotranscriptional RNA structure formation.RNA (New York, N.Y.) · 2013Review
- Mss116p: a DEAD-box protein facilitates RNA folding.RNA biology · 2013Review
- Kinetic analysis of pre-ribosome structure in vivo.RNA (New York, N.Y.) · 2012Article
- Transient RNA-protein interactions in RNA folding.The FEBS journal · 2011Review
- Proteins with RNA chaperone activity: a world of diverse proteins with a common task-impediment of RNA misfolding.Biochemistry research international · 2011Article
- Compact intermediates in RNA folding.Annual review of biophysics · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Efficient splicing of the td group I intron in vivo is dependent on the ribosome. In the absence of translation, the pre-mRNA is trapped in nonnative-splicing-incompetent conformations. Alternatively, folding of the pre-mRNA can be promoted by the RNA chaperone StpA or by the group I intron-specific splicing factor Cyt-18. To understand the mechanism of action of RNA chaperones, we probed the impact of StpA on the structure of the td intron in vivo. Our data suggest that StpA loosens tertiary interactions. The most prominent structural change was the opening of the base triples, which are involved in the correct orientation of the two major intron core domains. In line with the destabilizing activity of StpA, splicing of mutant introns with a reduced structural stability is sensitive to StpA. In contrast, Cyt-18 strengthens tertiary contacts, thereby rescuing splicing of structurally compromised td mutants in vivo. Our data provide direct evidence for protein-induced conformational changes within catalytic RNA in vivo. Whereas StpA resolves tertiary contacts enabling the RNA to refold, Cyt-18 contributes to the overall compactness of the td intron in vivo.
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Registered trials
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.