Evidence map›Paper›PMID 28521053›Full record

ArticleNucleic acids research2017

Compaction and condensation of DNA mediated by the C-terminal domain of Hfq.

Antoine Malabirade, Kai Jiang, Krzysztof Kubiak, Alvaro Diaz-Mendoza, Fan Liu, Jeroen A van Kan, Jean-François Berret, Véronique Arluison, Johan R C van der Maarel

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.7field-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

40 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  6. Effects of MgBiochemistry and biophysics reports · 2025
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  13. Interactions and Insertion ofInternational journal of molecular sciences · 2023
    Article
  14. Unraveling Membrane Perturbations Caused by the Bacterial Riboregulator Hfq.International journal of molecular sciences · 2022
    Article
  15. Three Microbial Musketeers of the Seas:International journal of molecular sciences · 2022
    Article
  16. Characterization of Bacterial Amyloids by Nano-infrared Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  17. Article
  18. Article
  19. Probing Amyloid-DNA Interaction with Nanofluidics.Methods in molecular biology (Clifton, N.J.) · 2022
    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

9 authors at 3 institutions in 3 countries.

Antoine MalabiradeLaboratoire Léon Brillouin, CEA, CNRS, Université Paris Saclay, 91191 Gif-sur-Yvette, France.
Kai JiangDepartment of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
Krzysztof KubiakLaboratoire Léon Brillouin, CEA, CNRS, Université Paris Saclay, 91191 Gif-sur-Yvette, France.
Alvaro Diaz-MendozaUniversité Paris Diderot, Sorbonne Paris Cité, 75013 Paris, France.
Fan LiuDepartment of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
Jeroen A van KanDepartment of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
Jean-François BerretUniversité Paris Diderot, Sorbonne Paris Cité, 75013 Paris, France.
Véronique ArluisonLaboratoire Léon Brillouin, CEA, CNRS, Université Paris Saclay, 91191 Gif-sur-Yvette, France.
Johan R C van der MaarelDepartment of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
National University of Singapore · SGCentre National de la Recherche Scientifique · FRDélégation Paris 7 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hfq is a bacterial protein that is involved in several aspects of nucleic acids metabolism. It has been described as one of the nucleoid associated proteins shaping the bacterial chromosome, although it is better known to influence translation and turnover of cellular RNAs. Here, we explore the role of Escherichia coli Hfq's C-terminal domain in the compaction of double stranded DNA. Various experimental methodologies, including fluorescence microscopy imaging of single DNA molecules confined inside nanofluidic channels, atomic force microscopy, isothermal titration microcalorimetry and electrophoretic mobility assays have been used to follow the assembly of the C-terminal and N-terminal regions of Hfq on DNA. Results highlight the role of Hfq's C-terminal arms in DNA binding, change in mechanical properties of the double helix and compaction of DNA into a condensed form. The propensity for bridging and compaction of DNA by the C-terminal domain might be related to aggregation of bound protein and may have implications for protein binding related gene regulation.

Indexed as

Gene Expression Regulation, BacterialBinding SitesChromosomes, BacterialDNADNA, BacterialElectrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsHost Factor 1 ProteinKineticsProtein AggregatesProtein BindingProtein DomainsThermodynamicsDNADNA, BacterialEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinProtein Aggregates

Identifiers

PMID28521053
PMCPMC5499573
OpenAlexW2613080661

What OpenQuestion holds

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LicenceCC BY-NC
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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.