ArticleNucleic acids research2005
Influence of RNA structural stability on the RNA chaperone activity of the Escherichia coli protein StpA.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Metabolic rearrangement enables adaptation of microbial growth rate to temperature shifts.Nature microbiology · 2025Article
- The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements.Nucleic acids research · 2021Article
- The Sac10b homolog from Sulfolobus islandicus is an RNA chaperone.Nucleic acids research · 2020Article
- 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
- Stability of local secondary structure determines selectivity of viral RNA chaperones.Nucleic acids research · 2018Article
- Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018Review
- DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Genetic and biochemical assays reveal a key role for replication restart proteins in group II intron retrohoming.PLoS genetics · 2013Article
- Protein roles in group I intron RNA folding: the tyrosyl-tRNA synthetase CYT-18 stabilizes the native state relative to a long-lived misfolded structure without compromising folding kinetics.Journal of molecular biology · 2010Article
- RNA misfolding and the action of chaperones.Frontiers in bioscience : a journal and virtual library · 2008Review
- Dissecting RNA chaperone activity.RNA (New York, N.Y.) · 2007Article
- Article
- RNA chaperone activity of L1 ribosomal proteins: phylogenetic conservation and splicing inhibition.Nucleic acids research · 2007Article
- RNA chaperone activity and RNA-binding properties of the E. coli protein StpA.Nucleic acids research · 2007Article
- Self-splicing of a group I intron reveals partitioning of native and misfolded RNA populations in yeast.RNA (New York, N.Y.) · 2006Article
- Computer simulation of chaperone effects of Archaeal C/D box sRNA binding on rRNA folding.Nucleic acids research · 2006Article
- Mechanisms of StpA-mediated RNA remodeling.RNA biologyReview
- Review
- RNA folding in living cells.RNA biologyReview
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins with RNA chaperone activity are able to promote folding of RNA molecules by loosening their structure. This RNA unfolding activity is beneficial when resolving misfolded RNA conformations, but could be detrimental to RNAs with low thermodynamic stability. In order to test this idea, we constructed various RNAs with different structural stabilities derived from the thymidylate synthase (td) group I intron and measured the effect of StpA, an Escherichia coli protein with RNA chaperone activity, on their splicing activity in vivo and in vitro. While StpA promotes splicing of the wild-type td intron and of mutants with wild-type-like stability, splicing of mutants with a lower structural stability is reduced in the presence of StpA. In contrast, splicing of an intron mutant, which is not destabilized but which displays a reduced population of correctly folded RNAs, is promoted by StpA. The sensitivity of an RNA towards StpA correlates with its structural stability. By lowering the temperature to 25 degrees C, a temperature at which the structure of these mutants becomes more stable, StpA is again able to stimulate splicing. These observations clearly suggest that the structural stability of an RNA determines whether the RNA chaperone activity of StpA is beneficial to folding.
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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.