ArticleRNA (New York, N.Y.)2002
Probing FinO-FinP RNA interactions by site-directed protein-RNA crosslinking and gelFRET.
Article in RNA (New York, N.Y.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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
20 citing papers in PubMed, 32 citations in OpenAlex.
- 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
- Isolation of nucleic acids using liquid-liquid phase separation of pH-sensitive elastin-like polypeptides.Scientific reports · 2024Article
- Biochemical and genetic dissection of the RNA-binding surface of the FinO domain ofRNA (New York, N.Y.) · 2023Article
- Biochemical and genetic dissection of the RNA-binding surface of the FinO domain ofbioRxiv : the preprint server for biology · 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
- Saturation mutagenesis charts the functional landscape of Salmonella ProQ and reveals a gene regulatory function of its C-terminal domain.Nucleic acids research · 2021Article
- 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
- Stability of local secondary structure determines selectivity of viral RNA chaperones.Nucleic acids research · 2018Article
- ProQ/FinO-domain proteins: another ubiquitous family of RNA matchmakers?Molecular microbiology · 2017Review
- Structure of theRNA (New York, N.Y.) · 2017Article
- Mapping interactions between the RNA chaperone FinO and its RNA targets.Nucleic acids research · 2011Article
- RNA chaperone activity and RNA-binding properties of the E. coli protein StpA.Nucleic acids research · 2007Article
- FinO is an RNA chaperone that facilitates sense-antisense RNA interactions.The EMBO journal · 2003Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The conjugative transfer of F-plasmids is repressed by a two-component system, which consists of the antisense RNA FinP and the protein FinO. FinO binds FinP, protecting it from endonucleolytic degradation and facilitating duplex formation between FinP and its complementary RNA. Here we present the results of site-specific protein-RNA cross-linking and gel-based fluorescence resonance energy transfer (gelFRET) experiments used to probe the structure of a complex of FinO bound to an RNA target consisting of a duplex with 5' and 3' single-stranded tails. The crosslinking experiments reveal that an extensive, largely positively charged surface on FinO contacts RNA. The gelFRET measurements indicate that the 5' single-stranded tail of the RNA is in closer contact with much of the protein than the distal, blunt end of the RNA duplex. These data suggest that significant conformational adjustments in the protein and/or the RNA accompany complex formation.
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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.