Evidence map›Paper›PMID 24516652›Full record

ArticlePloS one2014

ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.

Henrike Klinker, Felix Mueller-Planitz, Renliang Yang, Ignasi Forné, Chuan-Fa Liu, Lars Nordenskiöld, Peter B Becker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.Nature structural & molecular biology · 2024
    Article
  2. Article
  3. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.bioRxiv : the preprint server for biology · 2023
    Article
  4. Article
  5. Review
  6. Article
  7. In silico evidence for sequence-dependent nucleosome sliding.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Review
  9. Article
  10. Review
  11. Computational study of remodeling in a nucleosomal array.The European physical journal. E, Soft matter · 2015
    Article
  12. Article
  13. Review
  14. 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

7 authors at 3 institutions in 2 countries.

Henrike KlinkerDepartment of Molecular Biology, Adolf Butenandt Institut, Ludwig-Maximilians-Universität München, Munich, Germany ; Center for Integrated Protein Science Munich, Munich, Germany.
Felix Mueller-PlanitzDepartment of Molecular Biology, Adolf Butenandt Institut, Ludwig-Maximilians-Universität München, Munich, Germany.
Renliang YangSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Ignasi FornéCenter for Integrated Protein Science Munich, Munich, Germany ; Protein Analysis Unit, Adolf Butenandt Institut, Ludwig-Maximilians-Universität München, Munich, Germany.
Chuan-Fa LiuSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Lars NordenskiöldSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Peter B BeckerDepartment of Molecular Biology, Adolf Butenandt Institut, Ludwig-Maximilians-Universität München, Munich, Germany ; Center for Integrated Protein Science Munich, Munich, Germany.
Center for Integrated Protein Science Munich · DENanyang Technological University · SGLudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ISWI is the catalytic subunit of several ATP-dependent chromatin remodelling factors that catalyse the sliding of nucleosomes along DNA and thereby endow chromatin with structural flexibility. Full activity of ISWI requires residues of a basic patch of amino acids in the N-terminal 'tail' of histone H4. Previous studies employing oligopeptides and mononucleosomes suggested that acetylation of the H4 tail at lysine 16 (H4K16) within the basic patch may inhibit the activity of ISWI. On the other hand, the acetylation of H4K16 is known to decompact chromatin fibres. Conceivably, decompaction may enhance the accessibility of nucleosomal DNA and the H4 tail for ISWI interactions. Such an effect can only be evaluated at the level of nucleosome arrays. We probed the influence of H4K16 acetylation on the ATPase and nucleosome sliding activity of Drosophila ISWI in the context of defined, in vitro reconstituted chromatin fibres with physiological nucleosome spacing and linker histone content. Contrary to widespread expectations, the acetylation did not inhibit ISWI activity, but rather stimulated ISWI remodelling under certain conditions. Therefore, the effect of H4K16 acetylation on ISWI remodelling depends on the precise nature of the substrate.

Indexed as

Chromatin Assembly and DisassemblyAcetylationAdenosine TriphosphatasesAnimalsChromatinDrosophila melanogasterHistonesLysineMultiprotein ComplexesNucleosomesTranscription FactorsAdenosine TriphosphatasesChromatinHistonesISWI proteinLysineMultiprotein ComplexesNucleosomesTranscription Factors

Identifiers

PMID24516652
PMCPMC3916430
OpenAlexW2130830586

What OpenQuestion holds

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LicenceCC BY
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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.