Evidence map›Paper›PMID 25147238›Full record

ArticleRNA (New York, N.Y.)2014

Clostridium difficile Hfq can replace Escherichia coli Hfq for most of its function.

Joel Caillet, Céline Gracia, Fanette Fontaine, Eliane Hajnsdorf

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023
    Article
  5. Article
  6. Article
  7. An RNA-centric global view ofProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. 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
  9. Article
  10. Hfq: the flexible RNA matchmaker.Current opinion in microbiology · 2016
    Review
  11. Article
  12. Article
  13. 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 1 institution in 1 country.

Joel CailletCNRS FRE3630 (previously UPR9073), University Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 75005 Paris, France.
Céline GraciaCNRS FRE3630 (previously UPR9073), University Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 75005 Paris, France.
Fanette FontaineCNRS FRE3630 (previously UPR9073), University Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 75005 Paris, France.
Eliane HajnsdorfCNRS FRE3630 (previously UPR9073), University Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 75005 Paris, France eliane.hajnsdorf@ibpc.fr.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A gene for the Hfq protein is present in the majority of sequenced bacterial genomes. Its characteristic hexameric ring-like core structure is formed by the highly conserved N-terminal regions. In contrast, the C-terminal forms an extension, which varies in length, lacks homology, and is predicted to be unstructured. In Gram-negative bacteria, Hfq facilitates the pairing of sRNAs with their mRNA target and thus affects gene expression, either positively or negatively, and modulates sRNA degradation. In Gram-positive bacteria, its role is still poorly characterized. Numerous sRNAs have been detected in many Gram-positive bacteria, but it is not yet known whether these sRNAs act in association with Hfq. Compared with all other Hfqs, the C. difficile Hfq exhibits an unusual C-terminal sequence with 75% asparagine and glutamine residues, while the N-terminal core part is more conserved. To gain insight into the functionality of the C. difficile Hfq (Cd-Hfq) protein in processes regulated by sRNAs, we have tested the ability of Cd-Hfq to fulfill the functions of the E. coli Hfq (Ec-Hfq) by examining various functions associated with Hfq in both positive and negative controls of gene expression. We found that Cd-Hfq substitutes for most but not all of the tested functions of the Ec-Hfq protein. We also investigated the role of the C-terminal part of the Hfq proteins. We found that the C-terminal part of both Ec-Hfq and Cd-Hfq is not essential but contributes to some functions of both the E. coli and C. difficile chaperons.

Indexed as

Protein Biosynthesisbeta-GalactosidaseClostridioides difficileElectrophoretic Mobility Shift AssayEscherichia coliGene Expression Regulation, BacterialHost Factor 1 ProteinPhenotypeProtein BindingRNA, BacterialRNA, Messengerbeta-GalactosidaseHost Factor 1 ProteinRNA, BacterialRNA, MessengerClostridium difficileEscherichia coligene expressionHfqsmall noncoding RNAs

Identifiers

PMID25147238
PMCPMC4174439
OpenAlexW2161212397

What OpenQuestion holds

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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.