Evidence map›Paper›PMID 29850894›Full record

ArticleNucleic acids research2018

The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome.

Joshua M Tokuda, Ren Ren, Robert F Levendosky, Rebecca J Tay, Ming Yan, Lois Pollack, Gregory D Bowman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Solution conformational differences between conventional and CENP-A nucleosomes are accentuated by reversible deformation under high pressure.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
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  10. Article
  11. Review
  12. Review
  13. Torsional stress can regulate the unwrapping of two outer half superhelical turns of nucleosomal DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Nucleosome structure and dynamics are coming of age.Nature structural & molecular biology · 2019
    Review
  18. 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 2 institutions in 1 country.

Joshua M TokudaSchool of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853 USA.
Ren RenT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218 USA.
Robert F LevendoskyT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218 USA.
Rebecca J TayT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218 USA.
Ming YanT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218 USA.
Lois PollackSchool of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853 USA.
Gregory D BowmanT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218 USA.
Johns Hopkins University · USCornell University · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
Structural and Functional Characterization of the Chd1 Chromatin RemodelerR01GM084192 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BOWMAN, GREGORY DEAN · 2008 to 2024
$6.3M
Nucleic acid interactions with partners: ions and proteinsR35GM122514 · NIGMS · CORNELL UNIVERSITY · PI Lois Pollack · 2017 to 2026
$3.8M
Information Fusion in Biomolecular Structure and Motion DeterminationR01GM113240 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CHIRIKJIAN, GREGORY · 2014 to 2018
$1.9M
NIGMS NIH HHS R01 GM084192NIGMS NIH HHS R01 GM113240NIGMS NIH HHS R35 GM122514NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

Chromatin remodelers are ATP-dependent motors that reorganize DNA packaging by disrupting canonical histone-DNA contacts within the nucleosome. Here, we show that the Chd1 chromatin remodeler stimulates DNA unwrapping from the edge of the nucleosome in a nucleotide-dependent and DNA sequence-sensitive fashion. Nucleosome binding, monitored by stopped flow, was complex and sensitive to nucleotide, with AMP-PNP promoting faster binding than ADP·BeF3-. Nucleosome unwrapping by Chd1, examined by bulk FRET, occurred in the presence and absence of nucleotide and did not require the Chd1 DNA-binding domain. In AMP-PNP conditions, Chd1 unwrapped one side of the Widom 601 DNA more easily than the other, consistent with previous observations of 601 asymmetry and indicating that Chd1 amplifies intrinsic sequence properties of nucleosomal DNA. Using small angle X-ray scattering (SAXS) with contrast variation, we found distinct DNA conformations depending on the nucleotide analog bound to Chd1: with AMP-PNP, DNA primarily unwrapped in-plane with the nucleosomal disk, whereas with ADP·BeF3-, a significant fraction showed distinctive out-of-plane unwrapping as well. Taken together, our findings show tight coupling between entry/exit DNA of the nucleosome and the Chd1 ATPase motor, suggesting that dynamic nucleosome unwrapping is coupled to nucleosome binding and remodeling by Chd1.

Indexed as

Chromatin Assembly and DisassemblyDNA-Binding ProteinsDNA, FungalFluorescence Resonance Energy TransferNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsScattering, Small AngleX-Ray DiffractionCHD1 protein, S cerevisiaeDNA-Binding ProteinsDNA, FungalNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID29850894
PMCPMC6007315
OpenAlexW2792664778

What OpenQuestion holds

Textmetadata
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.