Evidence map›Paper›PMID 23804244›Full record

ArticleRNA (New York, N.Y.)2013

Hfq binding changes the structure of

Charlotte A Henderson, Helen A Vincent, Alessandra Casamento, Carlanne M Stone, Jack O Phillips, Peter D Cary, Frank Sobott, Darren M Gowers, James E N Taylor, Anastasia J Callaghan

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  8. Engineering a Circular Riboregulator inBiodesign research · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. Article
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  14. Review
  15. Article
  16. C-terminal domain of the RNA chaperone Hfq drives sRNA competition and release of target RNA.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Hfq: the flexible RNA matchmaker.Current opinion in microbiology · 2016
    Review
  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

10 authors at 2 institutions in 1 country.

Charlotte A HendersonBiophysics Laboratories, School of Biological Sciences, Institute of Biomedical and Biomolecular Sciences, University of Portsmouth, Portsmouth, PO1 2DT, United Kingdom.
Helen A Vincent
Alessandra Casamento
Carlanne M Stone
Jack O Phillips
Peter D Cary
Frank Sobott
Darren M Gowers
James E N Taylor
Anastasia J Callaghan
University of Portsmouth · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F013140/1
6 · The paper itself

Abstract

OxyS and RprA are two small noncoding RNAs (sRNAs) that modulate the expression of rpoS, encoding an alternative sigma factor that activates transcription of multiple Escherichia coli stress-response genes. While RprA activates rpoS for translation, OxyS down-regulates the transcript. Crucially, the RNA binding protein Hfq is required for both sRNAs to function, although the specific role played by Hfq remains unclear. We have investigated RprA and OxyS interactions with Hfq using biochemical and biophysical approaches. In particular, we have obtained the molecular envelopes of the Hfq-sRNA complexes using small-angle scattering methods, which reveal key molecular details. These data indicate that Hfq does not substantially change shape upon complex formation, whereas the sRNAs do. We link the impact of Hfq binding, and the sRNA structural changes induced, to transcript stability with respect to RNase E degradation. In light of these findings, we discuss the role of Hfq in the opposing regulatory functions played by RprA and OxyS in rpoS regulation.

Indexed as

Bacterial ProteinsBase SequenceBinding SitesBiophysical PhenomenaEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialHost Factor 1 ProteinModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein Structure, QuaternaryRepressor ProteinsRNA, BacterialRNA, Small UntranslatedRNA StabilityBacterial ProteinsEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinoxyS small RNA, E coliRepressor ProteinsRNA, BacterialRNA, Small UntranslatedSigma Factorsigma factor KatF protein, BacteriaHfqOxySrpoSRprAsRNA

Identifiers

PMID23804244
PMCPMC3708529
OpenAlexW2108502374

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.