ArticleNucleic acids research2011
Mapping interactions between the RNA chaperone FinO and its RNA targets.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 42 citations in OpenAlex.
- A Two-Step Purification Strategy for RNA and RNA-Protein Complexes for Crystallization.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Different RNA recognition by ProQ and FinO depends on the sequence surrounding intrinsic terminator hairpins.RNA (New York, N.Y.) · 2025Article
- RNA recognition by minimal ProQ fromRNA (New York, N.Y.) · 2025Article
- Biochemical and genetic dissection of the RNA-binding surface of the FinO domain ofRNA (New York, N.Y.) · 2023Article
- 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
- Characterization of a Novel Carbapenem-Resistant Klebsiella michiganensis Strain Coharboring the blaCurrent microbiology · 2022Article
- Towards a better understanding of antimicrobial resistance dissemination: what can be learnt from studying model conjugative plasmids?Military Medical Research · 2022Review
- 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
- Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity.Frontiers in cellular and infection 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
- Determinants of RNA recognition by the FinO domain of the Escherichia coli ProQ protein.Nucleic acids research · 2020Article
- Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ.Nucleic acids research · 2020Article
- Coupled Transcription-Translation in Prokaryotes: An Old Couple With New Surprises.Frontiers in microbiology · 2020Review
- AtxA-Controlled Small RNAs ofFrontiers in microbiology · 2020Article
- Posttranscription Initiation Control of Gene Expression Mediated by Bacterial RNA-Binding Proteins.Annual review of microbiology · 2019Review
- Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factors.BMC genomics · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Bacterial conjugation is regulated by two-component repression comprising the antisense RNA FinP, and its protein co-factor FinO. FinO mediates base-pairing of FinP to the 5'-untranslated region (UTR) of traJ mRNA, which leads to translational inhibition of the transcriptional activator TraJ and subsequent down regulation of conjugation genes. Yet, little is known about how FinO binds to its RNA targets or how this interaction facilitates FinP and traJ mRNA pairing. Here, we use solution methods to determine how FinO binds specifically to its minimal high affinity target, FinP stem-loop II (SLII), and its complement SLIIc from traJ mRNA. Ribonuclease footprinting reveals that FinO contacts the base of the stem and the 3' single-stranded tails of these RNAs. The phosphorylation or oxidation of the 3'-nucleotide blocks FinO binding, suggesting FinO binds the 3'-hydroxyl of its RNA targets. The collective results allow the generation of an energy-minimized model of the FinO-SLII complex, consistent with small-angle X-ray scattering data. The repression complex model was constrained using previously reported cross-linking data and newly developed footprinting results. Together, these data lead us to propose a model of how FinO mediates FinP/traJ mRNA pairing to down regulate bacterial conjugation.
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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.