Evidence map›Paper›PMID 25404287›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structural model of an mRNA in complex with the bacterial chaperone Hfq.

Yi Peng, Joseph E Curtis, Xianyang Fang, Sarah A Woodson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Effect ofInternational journal of microbiology · 2025
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  5. Small-Angle X-Ray Scattering for Macromolecular Complexes.Advances in experimental medicine and biology · 2024
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Specific and Global RNA Regulators inInternational journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity.Frontiers in cellular and infection microbiology · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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

4 authors at 3 institutions in 1 country.

Yi PengCell, Molecular and Developmental Biology and Biophysics Program, Johns Hopkins University, Baltimore, MD 21218;
Joseph E CurtisCenter for Neutron Research, National Institute of Standards and Technology, Gaithersburg, MD 20899;
Xianyang FangStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702; and.
Sarah A WoodsonT. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218 swoodson@jhu.edu.
Johns Hopkins University · USCenter for Cancer Research · USNIST Center for Neutron Research · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
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 GM46686NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

The Sm-like protein Hfq (host factor Q-beta phage) facilitates regulation by bacterial small noncoding RNAs (sRNAs) in response to stress and other environmental signals. Here, we present a low-resolution model of Escherichia coli Hfq bound to the rpoS mRNA, a bacterial stress response gene that is targeted by three different sRNAs. Selective 2'-hydroxyl acylation and primer extension, small-angle X-ray scattering, and Monte Carlo molecular dynamics simulations show that the distal face and lateral rim of Hfq interact with three sites in the rpoS leader, folding the RNA into a compact tertiary structure. These interactions are needed for sRNA regulation of rpoS translation and position the sRNA target adjacent to an sRNA binding region on the proximal face of Hfq. Our results show how Hfq specifically distorts the structure of the rpoS mRNA to enable sRNA base pairing and translational control.

Indexed as

Escherichia coli ProteinsHost Factor 1 ProteinMolecular Dynamics SimulationMonte Carlo MethodNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRNA, BacterialRNA, MessengerRNA, Small UntranslatedScattering, Small AngleSigma FactorX-Ray DiffractionEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinRNA, BacterialRNA, MessengerRNA, Small UntranslatedSigma Factorbacterial posttranscriptional controlLsm proteinRNA–protein interactionsSAXSsmall noncoding RNA

Identifiers

PMID25404287
PMCPMC4260595
OpenAlexW2108438522

What OpenQuestion holds

Textmetadata
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.