Evidence map›Paper›PMID 23771143›Full record

ArticleNucleic acids research2013

Conserved arginines on the rim of Hfq catalyze base pair formation and exchange.

Subrata Panja, Daniel J Schu, Sarah A Woodson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
10.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

78 citing papers in PubMed, 121 citations in OpenAlex.

  1. Journal of molecular biology · 2026
    Article
  2. Article
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  5. Competition for Hfq drives kinetic selection of mRNA targets byProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. What makes a small RNA work?Nucleic acids research · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
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  12. Article
  13. An acetyltranferase moonlights as a regulator of the RNA binding repertoire of the RNA chaperone Hfq inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Article
  20. Article

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Subrata PanjaT.C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA and Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892-5430, USA.
Daniel J Schu
Sarah A Woodson
MRC Laboratory of Molecular Biology · GB

Funding

Role of Exon Structure in Splicing of Group I IntronsR01GM046686 · NIGMS · UNIVERSITY OF MARYLAND COLLEGE PK CAMPUS · PI WOODSON, SARAH A. · 1992 to 2014
$4.0M
NIGMS NIH HHS R01 GM046686NIGMS NIH HHS R01 GM46686
6 · The paper itself

Abstract

The Sm-like protein Hfq is required for gene regulation by small RNAs (sRNAs) in bacteria and facilitates base pairing between sRNAs and their mRNA targets. The proximal and distal faces of the Hfq hexamer specifically bind sRNA and mRNA targets, but they do not explain how Hfq accelerates the formation and exchange of RNA base pairs. Here, we show that conserved arginines on the outer rim of the hexamer that are known to interact with sRNA bodies are required for Hfq's chaperone activity. Mutations in the arginine patch lower the ability of Hfq to act in sRNA regulation of rpoS translation and eliminate annealing of natural sRNAs or unstructured oligonucleotides, without preventing binding to either the proximal or distal face. Stopped-flow FRET and fluorescence anisotropy show that complementary RNAs transiently form a ternary complex with Hfq, but the RNAs are not released as a double helix in the absence of rim arginines. RNAs bound to either face of Hfq quench the fluorescence of a tryptophan adjacent to the arginine patch, demonstrating that the rim can simultaneously engage two RNA strands. We propose that the arginine patch overcomes entropic and electrostatic barriers to helix nucleation and constitutes the active site for Hfq's chaperone function.

Indexed as

Base PairingArginineBacterial ProteinsBase SequenceCatalytic DomainConserved SequenceEscherichia coli ProteinsHost Factor 1 ProteinLysineMutationNucleic Acid ConformationProtein BindingProtein BiosynthesisRNA, BacterialRNA FoldingRNA, MessengerArginineBacterial ProteinsEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinLysineRNA, BacterialRNA, MessengerRNA, Small UntranslatedSigma Factorsigma factor KatF protein, Bacteria

Identifiers

PMID23771143
PMCPMC3753642
OpenAlexW1967408259

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.