Evidence map›Paper›PMID 34643712›Full record

ArticleNucleic acids research2021

Structural basis of chromatin regulation by histone variant H2A.Z.

Tyler S Lewis, Vladyslava Sokolova, Harry Jung, Honkit Ng, Dongyan Tan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Histone Variant H2A.Z Enhances Histone and Nucleosome Dynamics.Molecular & cellular proteomics : MCP · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. IMPACTS OF DNA METHYLATION ON H2A.Z DEPOSITION AND NUCLEOSOME STABILITY.bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. The shifting paradigm of chromatin structure: from the 30-nm chromatin fiber to liquid-like organization.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Review
  16. Article
  17. DDM1 Maintains Heterochromatin by Regulating Histone Variants.International journal of molecular sciences · 2025
    Review
  18. Article
  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

5 authors at 2 institutions in 1 country.

Tyler S LewisDepartment of Pharmacological Sciences, Stony Brook University; Stony Brook, NY 11794, USA.
Vladyslava SokolovaDepartment of Pharmacological Sciences, Stony Brook University; Stony Brook, NY 11794, USA.
Harry JungDepartment of Pharmacological Sciences, Stony Brook University; Stony Brook, NY 11794, USA.
Honkit NgDepartment of Pharmacological Sciences, Stony Brook University; Stony Brook, NY 11794, USA.
Dongyan TanDepartment of Pharmacological Sciences, Stony Brook University; Stony Brook, NY 11794, USA.ORCID 0000-0002-6796-6745
Stony Brook University · USNew York Proton Center · US

Funding

Pacific Northwest Center for Cryo-EM - Screening supplementU24GM129547 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI EVANS, JAMES E, GOUAUX, JAMES E · 2018 to 2023
$54.8M
Dynamics and Regulation of Chromatin in DNA MetabolismR35GM133611 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI TAN, DONGYAN · 2019 to 2023
$2.1M
A 200KV CRYO-TEM FOR IMAGING BIOLOGICAL STRUCTURESS10OD012272 · OD · STATE UNIVERSITY NEW YORK STONY BROOK · PI NEIMAN, AARON M · 2015 to 2015
$2.0M
NIGMS NIH HHS R35 GM133611NIGMS NIH HHS U24 GM129547NIH HHS S10 OD012272
6 · The paper itself

Abstract

The importance of histone variant H2A.Z in transcription regulation has been well established, yet its mechanism-of-action remains enigmatic. Conflicting evidence exists in support of both an activating and a repressive role of H2A.Z in transcription. Here we report cryo-electron microscopy (cryo-EM) structures of nucleosomes and chromatin fibers containing H2A.Z and those containing canonical H2A. The structures show that H2A.Z incorporation results in substantial structural changes in both nucleosome and chromatin fiber. While H2A.Z increases the mobility of DNA terminus in nucleosomes, it simultaneously enables nucleosome arrays to form a more regular and condensed chromatin fiber. We also demonstrated that H2A.Z's ability to enhance nucleosomal DNA mobility is largely attributed to its characteristic shorter C-terminus. Our study provides the structural basis for H2A.Z-mediated chromatin regulation, showing that the increase flexibility of the DNA termini in H2A.Z nucleosomes is central to its dual-functions in chromatin regulation and in transcription.

Indexed as

Chromatin Assembly and DisassemblyAmino Acid SequenceAnimalsBinding SitesCloning, MolecularCryoelectron MicroscopyDNAEscherichia coliGene ExpressionGene Expression RegulationGenetic VectorsHistonesMiceModels, MolecularNucleosomesProtein BindingDNAH2az1 protein, mouseHistonesNucleosomesRecombinant Proteins

Identifiers

PMID34643712
PMCPMC8565303
OpenAlexW3207804469

What OpenQuestion holds

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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.