Evidence map›Paper›PMID 22718981›Full record

ArticleNucleic acids research2012

Structural flexibility of RNA as molecular basis for Hfq chaperone function.

Euripedes de Almeida Ribeiro, Mads Beich-Frandsen, Petr V Konarev, Weifeng Shang, Branislav Vecerek, Georg Kontaxis, Hermann Hämmerle, Herwig Peterlik, Dmitri I Svergun, Udo Bläsi and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Journal of molecular biology · 2026
    Article
  2. Specific and Global RNA Regulators inInternational journal of molecular sciences · 2021
    Review
  3. Article
  4. Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Hfq binding changes the structure ofRNA (New York, N.Y.) · 2013
    Article
  16. Article
  17. Article
  18. Article
  19. Cycling of RNAs on Hfq.RNA biology · 2013
    Review
  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

11 authors at 4 institutions in 3 countries.

Euripedes de Almeida RibeiroDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Mads Beich-Frandsen
Petr V Konarev
Weifeng Shang
Branislav Vecerek
Georg Kontaxis
Hermann Hämmerle
Herwig Peterlik
Dmitri I Svergun
Udo Bläsi
Kristina Djinović-Carugo
University of Ljubljana · SIUniversity of Vienna · ATMax Perutz Labs · ATVienna Biocenter · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In enteric bacteria, many small regulatory RNAs (sRNAs) associate with the RNA chaperone host factor Q (Hfq) and often require the protein for regulation of target mRNAs. Previous studies suggested that the hexameric Escherichia coli Hfq (Hfq(Ec)) binds sRNAs on the proximal site, whereas the distal site has been implicated in Hfq-mRNA interactions. Employing a combination of small angle X-ray scattering, nuclear magnetic resonance and biochemical approaches, we report the structural analysis of a 1:1 complex of Hfq(Ec) with a 34-nt-long subsequence of a natural substrate sRNA, DsrA (DsrA(34)). This sRNA is involved in post-transcriptional regulation of the E. coli rpoS mRNA encoding the stationary phase sigma factor RpoS. The molecular envelopes of Hfq(Ec) in complex with DsrA(34) revealed an overall asymmetric shape of the complex in solution with the protein maintaining its doughnut-like structure, whereas the extended DsrA(34) is flexible and displays an ensemble of different spatial arrangements. These results are discussed in terms of a model, wherein the structural flexibility of RNA ligands bound to Hfq stochastically facilitates base pairing and provides the foundation for the RNA chaperone function inherent to Hfq.

Indexed as

Escherichia coli ProteinsHost Factor 1 ProteinLightModels, MolecularNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationProtein BindingRNA, Small UntranslatedScattering, RadiationScattering, Small AngleX-Ray DiffractionDsrA RNA, E coliEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinRNA, Small Untranslated

Identifiers

PMID22718981
PMCPMC3439903
OpenAlexW2032316604

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.