Evidence map›Paper›PMID 35173352›Full record

ArticleNature structural & molecular biology2022

Nucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state.

Ilana M Nodelman, Sayan Das, Anneliese M Faustino, Stephen D Fried, Gregory D Bowman, Jean-Paul Armache

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.2field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Beyond the mono-nucleosome.Biochemical Society transactions · 2025
    Review
  16. Article
  17. Article
  18. How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024
    Review
  19. 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

6 authors at 2 institutions in 1 country.

Ilana M Nodelman *Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD, USA.ORCID http://orcid.org/0000-0003-1181-6913
Sayan Das *Department of Biochemistry and Molecular Biology and the Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, PA, USA.ORCID http://orcid.org/0000-0002-8925-6832
Anneliese M FaustinoDepartment of Chemistry, Johns Hopkins University, Baltimore, MD, USA.ORCID http://orcid.org/0000-0003-1743-9186
Stephen D FriedThomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD, USA.ORCID http://orcid.org/0000-0003-2494-2193
Gregory D BowmanThomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD, USA. gdbowman@jhu.edu.ORCID http://orcid.org/0000-0001-8025-4315
Jean-Paul ArmacheDepartment of Biochemistry and Molecular Biology and the Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, PA, USA. jparmache@psu.edu.ORCID http://orcid.org/0000-0001-9195-2282
Johns Hopkins University · USPennsylvania State University · US

Funding

Structural and Functional Characterization of the Chd1 Chromatin RemodelerR01GM084192 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BOWMAN, GREGORY DEAN · 2008 to 2024
$6.3M
Watching Proteins Fold (or Misfold) in vivo with Mass SpectrometryDP2GM140926 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FRIED, STEPHEN DAVID · 2020 to 2020
$2.3M
NCI NIH HHS HHSN261200800001ENIGMS NIH HHS DP2 GM140926NIGMS NIH HHS R01 GM084192
6 · The paper itself

Abstract

Chromatin remodelers are ATP-dependent enzymes that reorganize nucleosomes within all eukaryotic genomes. Here we report a complex of the Chd1 remodeler bound to a nucleosome in a nucleotide-free state, determined by cryo-EM to 2.3 Å resolution. The remodeler stimulates the nucleosome to absorb an additional nucleotide on each strand at two different locations: on the tracking strand within the ATPase binding site and on the guide strand one helical turn from the ATPase motor. Remarkably, the additional nucleotide on the tracking strand is associated with a local transformation toward an A-form geometry, explaining how sequential ratcheting of each DNA strand occurs. The structure also reveals a histone-binding motif, ChEx, which can block opposing remodelers on the nucleosome and may allow Chd1 to participate in histone reorganization during transcription.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceBinding SitesChromatin Assembly and DisassemblyCryoelectron MicroscopyDNA-Binding ProteinsDNA, FungalModels, BiologicalModels, MolecularMolecular Motor ProteinsNucleosomesNucleotidesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCHD1 protein, S cerevisiaeDNA-Binding ProteinsDNA, FungalMolecular Motor ProteinsNucleosomesNucleotidesSaccharomyces cerevisiae Proteins

Identifiers

PMID35173352
PMCPMC9107065
OpenAlexW4213190051

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.