Evidence map›Paper›PMID 24086160›Full record

ArticlePLoS genetics2013

Binding of NF-κB to nucleosomes: effect of translational positioning, nucleosome remodeling and linker histone H1.

Imtiaz Nisar Lone, Manu Shubhdarshan Shukla, John Lalith Charles Richard, Zahary Yordanov Peshev, Stefan Dimitrov, Dimitar Angelov

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  9. Article
  10. NF-κB Rel subunit exchange on a physiological timescale.Protein science : a publication of the Protein Society · 2021
    Article
  11. Transcription factor NF-κB unravels nucleosomes.Biochimica et biophysica acta. General subjects · 2021
    Article
  12. Article
  13. TheCancer research · 2021
    Article
  14. Review
  15. Article
  16. Article
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  18. Article
  19. Pioneer factors and their in vitro identification methods.Molecular genetics and genomics : MGG · 2020
    Review
  20. Review
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

6 authors at 4 institutions in 2 countries.

Imtiaz Nisar LoneUniversité de Lyon, Laboratoire de Biologie Moléculaire de la Cellule, CNRS-UMR 5239, Ecole Normale Supérieure de Lyon, Lyon, France.
Manu Shubhdarshan Shukla
John Lalith Charles Richard
Zahary Yordanov Peshev
Stefan Dimitrov
Dimitar Angelov
Centre National de la Recherche Scientifique · FRInstitut pour l'avancée des biosciences · FRÉcole Normale Supérieure de Lyon · FRUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NF-κB is a key transcription factor regulating the expression of inflammatory responsive genes. How NF-κB binds to naked DNA templates is well documented, but how it interacts with chromatin is far from being clear. Here we used a combination of UV laser footprinting, hydroxyl footprinting and electrophoretic mobility shift assay to investigate the binding of NF-κB to nucleosomal templates. We show that NF-κB p50 homodimer is able to bind to its recognition sequence, when it is localized at the edge of the core particle, but not when the recognition sequence is at the interior of the nucleosome. Remodeling of the nucleosome by the chromatin remodeling machine RSC was not sufficient to allow binding of NF-κB to its recognition sequence located in the vicinity of the nucleosome dyad, but RSC-induced histone octamer sliding allowed clearly detectable binding of NF-κB with the slid particle. Importantly, nucleosome dilution-driven removal of H2A-H2B dimer led to complete accessibility of the site located close to the dyad to NF-κB. Finally, we found that NF-κB was able to displace histone H1 and prevent its binding to nucleosome. These data provide important insight on the role of chromatin structure in the regulation of transcription of NF-κB dependent genes.

Indexed as

Protein BiosynthesisAnimalsBinding SitesChromatinDimerizationDNA-Binding ProteinsHistonesMi-2 Nucleosome Remodeling and Deacetylase ComplexNF-kappa BNucleosomesProtein BindingUltraviolet RaysXenopusChromatinDNA-Binding ProteinsHistonesMi-2 Nucleosome Remodeling and Deacetylase ComplexNF-kappa BNucleosomes

Identifiers

PMID24086160
PMCPMC3784511
OpenAlexW2022328060

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.