Evidence map›Paper›PMID 25684208›Full record

ArticleMolecular cell2015

A nucleotide-driven switch regulates flanking DNA length sensing by a dimeric chromatin remodeler.

John D Leonard, Geeta J Narlikar

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.2field-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

48 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  9. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.Nature structural & molecular biology · 2024
    Article
  10. Article
  11. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.bioRxiv : the preprint server for biology · 2023
    Article
  12. Article
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  14. Cryo-EM structure of the human Sirtuin 6-nucleosome complex.bioRxiv : the preprint server for biology · 2023
    Article
  15. Article
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  18. Review
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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

2 authors at 1 institution in 1 country.

John D LeonardDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA; Tetrad Graduate Program, University of California, San Francisco, San Francisco, CA 94158, USA.
Geeta J NarlikarDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: geeta.narlikar@ucsf.edu.
University of California, San Francisco · US

Funding

Mechanistic Analysis of Chromatin RemodelingR01GM073767 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI NARLIKAR, GEETA J · 2005 to 2018
$4.7M
NIGMS NIH HHS GM073767NIGMS NIH HHS R01 GM073767
6 · The paper itself

Abstract

The ATP-dependent chromatin assembly factor (ACF) spaces nucleosomes to promote formation of silent chromatin. Two copies of its ATPase subunit SNF2h bind opposite sides of a nucleosome, but how these protomers avoid competition is unknown. SNF2h senses the length of DNA flanking a nucleosome via its HAND-SANT-SLIDE (HSS) domain, yet it is unclear how this interaction enhances remodeling. Using covalently connected SNF2h dimers we show that dimerization accelerates remodeling and that the HSS contributes to communication between protomers. We further identify a nucleotide-dependent conformational change in SNF2h. In one conformation the HSS binds flanking DNA, and in another conformation the HSS engages the nucleosome core. Based on these results, we propose a model in which DNA length sensing and translocation are performed by two distinct conformational states of SNF2h. Such separation of function suggests that these activities could be independently regulated to affect remodeling outcomes.

Indexed as

Chromatin Assembly and DisassemblyAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceBromodomain Containing ProteinsChromatinChromosomal Proteins, Non-HistoneDNAFluorescence Resonance Energy TransferFluorescent DyesModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationNucleosomesAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateBAZ1A protein, humanBromodomain Containing ProteinsChromatinChromosomal Proteins, Non-HistoneDNAFluorescent DyesNucleosomesNucleotidesSMARCA5 protein, humanTranscription Factors

Identifiers

PMID25684208
PMCPMC4355161
OpenAlexW2053322986

What OpenQuestion holds

Textmetadata
LicenceTDM
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.