Evidence map›Paper›PMID 31575967›Full record

ArticleScientific reports2019

Identification of protein-protein and ribonucleoprotein complexes containing Hfq.

Joël Caillet, Bruno Baron, Irina V Boni, Célia Caillet-Saguy, Eliane Hajnsdorf

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. A bacterial translation activator with an intrinsically disordered RNA-binding region.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. New Regulatory roles for Human Serum Amyloid A.International journal of research in oncology · 2024
    Article
  8. 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
  9. Article
  10. CsrA Shows Selective Regulation of sRNA-mRNA Networks.bioRxiv : the preprint server for biology · 2023
    Article
  11. CsrA selectively modulates sRNA-mRNA regulator outcomes.Frontiers in molecular biosciences · 2023
    Article
  12. Article
  13. Article
  14. A fluorescence-based genetic screen reveals diverse mechanisms silencing small RNA signaling inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Review
  16. Article
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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

5 authors at 4 institutions in 2 countries.

Joël CailletUMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, 75005, Paris, France.
Bruno BaronInstitut Pasteur, Plateforme de Biophysique Macromoléculaire, Center for Technical Resources and Research (C2RT), 25-28 rue du Dr Roux, 75724, Paris, cedex 15, France.
Irina V BoniShemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997, Moscow, Russia.
Célia Caillet-SaguyInstitut Pasteur, Laboratoire Récepteurs-Canaux, Département de Neuroscience, 25-28 rue du Dr Roux, 75724, Paris, cedex 15, France.
Eliane HajnsdorfUMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, 75005, Paris, France. Eliane.Hajnsdorf@ibpc.fr.
Laboratoire des Biomolécules · FRInstitut de Biologie Physico-Chimique · FRInstitute of Bioorganic Chemistry · RUUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hfq is a RNA-binding protein that plays a pivotal role in the control of gene expression in bacteria by stabilizing sRNAs and facilitating their pairing with multiple target mRNAs. It has already been shown that Hfq, directly or indirectly, interacts with many proteins: RNase E, Rho, poly(A)polymerase, RNA polymerase… In order to detect more Hfq-related protein-protein interactions we have used two approaches, TAP-tag combined with RNase A treatment to access the role of RNA in these complexes, and protein-protein crosslinking, which freezes protein-protein complexes formed in vivo. In addition, we have performed microscale thermophoresis to evaluate the role of RNA in some of the complexes detected and used far-western blotting to confirm some protein-protein interactions. Taken together, the results show unambiguously a direct interaction between Hfq and EF-Tu. However a very large number of the interactions of proteins with Hfq in E. coli involve RNAs. These RNAs together with the interacting protein, may play an active role in the formation of Hfq-containing complexes with previously unforeseen implications for the riboregulatory functions of Hfq.

Indexed as

Blotting, WesternEscherichia coliEscherichia coli ProteinsHost Factor 1 ProteinMultiprotein ComplexesRibonuclease, PancreaticRibonucleoproteinsEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinMultiprotein ComplexesRibonuclease, PancreaticRibonucleoproteins

Identifiers

PMID31575967
PMCPMC6773851
OpenAlexW2978597414

What OpenQuestion holds

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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.