ArticleThe EMBO journal2003
FinO is an RNA chaperone that facilitates sense-antisense RNA interactions.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 72 citations in OpenAlex.
- RNA recognition by minimal ProQ fromRNA (New York, N.Y.) · 2025Article
- Comprehensive analysis of Enterobacteriaceae IncX plasmids reveals robust conjugation regulators PrfaH, H-NS, and conjugation-fitness tradeoff.Communications biology · 2025Article
- FinO/ProQ-family proteins: an evolutionary perspective.Bioscience reports · 2023Review
- Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones.Nature communications · 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
- Saturation mutagenesis charts the functional landscape of Salmonella ProQ and reveals a gene regulatory function of its C-terminal domain.Nucleic acids research · 2021Article
- In vivo targets of Salmonella FinO include a FinP-like small RNA controlling copy number of a cohabitating plasmid.Nucleic acids research · 2021Article
- A ProQ/FinO family protein involved in plasmid copy number control favours fitness of bacteria carrying mcr-1-bearing IncI2 plasmids.Nucleic acids research · 2021Article
- Diversity and Versatility in Small RNA-Mediated Regulation in Bacterial Pathogens.Frontiers in microbiology · 2021Review
- Solution structure and RNA-binding of a minimal ProQ-homolog fromRNA (New York, N.Y.) · 2020Article
- Global discovery of bacterial RNA-binding proteins by RNase-sensitive gradient profiles reports a new FinO domain protein.RNA (New York, N.Y.) · 2020Article
- Protein Dynamics in F-like Bacterial Conjugation.Biomedicines · 2020Review
- The Sac10b homolog from Sulfolobus islandicus is an RNA chaperone.Nucleic acids research · 2020Article
- Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ.Nucleic acids research · 2020Article
- Modulation of Bacterial Fitness and Virulence Through Antisense RNAs.Frontiers in cellular and infection microbiology · 2020Review
- An RNA Chaperone-Like Protein Plays Critical Roles in Chloroplast mRNA Stability and Translation in Arabidopsis and Maize.The Plant cell · 2019Article
- Polynucleotide phosphorylase: Not merely an RNase but a pivotal post-transcriptional regulator.PLoS genetics · 2018Review
- Small Alarmone Synthetases as novel bacterial RNA-binding proteins.RNA biology · 2017Review
- Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factors.BMC genomics · 2017Article
- ProQ/FinO-domain proteins: another ubiquitous family of RNA matchmakers?Molecular microbiology · 2017Review
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
The protein FinO represses F-plasmid conjugative transfer by facilitating interactions between the mRNA of the major F-plasmid transcriptional activator, TraJ, and an antisense RNA, FinP. FinO is known to bind stem-loop structures in both FinP and traJ RNAs; however, the mechanism by which FinO facilitates sense-antisense pairing is poorly understood. Here we show that FinO acts as an RNA chaperone to promote strand exchange and duplexing between minimal RNA targets derived from FinP. This strongly suggests that FinO may function to destabilize internal secondary structures within FinP and traJ RNAs that would otherwise act as a kinetic trap to sense-antisense pairing. The energy for FinO-catalyzed base-pair destabilization does not arise from ATP hydrolysis but appears to be supplied directly from FinO RNA binding free energy. An analysis of the activities of mutants that are specifically deficient in strand exchange but not RNA-binding activity demonstrates that strand exchange is essential to the ability of FinO to mediate sense-antisense RNA recognition, and that this function also plays a role in repression of conjugation 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.