ArticleRNA (New York, N.Y.)2007
Dissecting RNA chaperone activity.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
82 citing papers in PubMed, 130 citations in OpenAlex.
- Identification of proteins exhibitingRNA biology · 2026Article
- DNA methylation enhances cooperative disentanglement by the Hfq nucleoid-associated protein.European biophysics journal : EBJ · 2026Article
- A Dual-Color Electrophoretic Mobility Shift Assay to Examine RNA-Binding and RNA Chaperone Activity Simultaneously.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The LARP6 La module fromRNA biology · 2025Article
- Structural flexibility in the ordered domain of the dengue virus strain 2 capsid protein is critical for chaperoning viral RNA replication.Cellular and molecular life sciences : CMLS · 2025Article
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.iScience · 2024Article
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.bioRxiv : the preprint server for biology · 2024Article
- Review
- Biochemical and genetic dissection of the RNA-binding surface of the FinO domain ofRNA (New York, N.Y.) · 2023Article
- Interactions and Insertion ofInternational journal of molecular sciences · 2023Article
- c-di-GMP regulates activity of the PlzA RNA chaperone from the Lyme disease spirochete.Molecular microbiology · 2023Article
- Article
- Dynamic Refolding of OxyS sRNA by the Hfq RNA Chaperone.Journal of molecular biology · 2022Article
- Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication inQRB discovery · 2022Article
- The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements.Nucleic acids research · 2021Article
- Kinetics of protein-assisted nucleic acid interconversion monitored by transient time resolved fluorescence in microfluidic droplets.Nucleic acids research · 2021Article
- Transcription complexes as RNA chaperones.Transcription · 2021Article
- Stepwise sRNA targeting of structured bacterial mRNAs leads to abortive annealing.Molecular cell · 2021Article
- An RNA pseudoknot is essential for standby-mediated translation of the tisB toxin mRNA in Escherichia coli.Nucleic acids research · 2020Article
- RNA-Binding Proteins Driving the Regulatory Activity of Small Non-coding RNAs in Bacteria.Frontiers in molecular biosciences · 2020Review
22 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many RNA-binding proteins help RNAs to fold via their RNA chaperone activity. This term has been used widely without accounting for the diversity of the observed reactions, which include complex events like restructuring of misfolded catalytic RNAs, promoting the assembly of RNA-protein complexes, and mediating RNA-RNA interactions. Proteins display very diverse activities depending on the assays used to measure RNA chaperone activity. To classify proteins with this activity, we compared three exemplary proteins from E. coli, host factor Hfq, ribosomal protein S1, and the histone-like protein StpA for their abilities to promote two simple reactions, RNA annealing and strand displacement. The results of a FRET-based assay show that S1 promotes only RNA strand displacement while Hfq solely enhances RNA annealing. StpA, in contrast, is active in both reactions. To test whether the two activities can be assigned to different domains of the bipartite-structured StpA, we assayed the purified N- and C- terminal domains separately. While both domains are unable to promote RNA annealing, we can attribute the RNA strand displacement activity of StpA to the C-terminal domain. Correlating with their RNA annealing activities, only Hfq and full-length StpA display simultaneous binding of two RNAs, suggesting a matchmaker-like model for this activity. For StpA, this "RNA crowding" requires protein-protein interactions, since a dimerization-deficient StpA mutant lost the ability to bind and anneal two RNAs. These results underline the difference between the two reaction types, making it necessary to distinguish and classify proteins according to their specific RNA chaperone activities.
Indexed as
Identifiers
What OpenQuestion holds
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.