Evidence map›Paper›PMID 26116819›Full record

ArticleeLife2015

H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement in budding yeast.

Anand Ranjan, Feng Wang, Gaku Mizuguchi, Debbie Wei, Yingzi Huang, Carl Wu

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Article
  2. Histone Variant H2A.Z Enhances Histone and Nucleosome Dynamics.Molecular & cellular proteomics : MCP · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Structure of the human TIP60 complex.Nature communications · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Structure and Function of Chromatin Remodelers.Journal of molecular biology · 2021
    Review
  18. Review
  19. Biophysics of Chromatin Remodeling.Annual review of biophysics · 2021
    Review
  20. Review
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.

Anand RanjanJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
Feng WangLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, United States.
Gaku MizuguchiJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
Debbie WeiLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, United States.
Yingzi HuangLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, United States.
Carl WuJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.

Funding

Howard Hughes Medical InstituteIntramural NIH HHS
6 · The paper itself

Abstract

The histone variant H2A.Z is a universal mark of gene promoters, enhancers, and regulatory elements in eukaryotic chromatin. The chromatin remodeler SWR1 mediates site-specific incorporation of H2A.Z by a multi-step histone replacement reaction, evicting histone H2A-H2B from the canonical nucleosome and depositing the H2A.Z-H2B dimer. Binding of both substrates, the canonical nucleosome and the H2A.Z-H2B dimer, is essential for activation of SWR1. We found that SWR1 primarily recognizes key residues within the α2 helix in the histone-fold of nucleosomal histone H2A, a region not previously known to influence remodeler activity. Moreover, SWR1 interacts preferentially with nucleosomal DNA at superhelix location 2 on the nucleosome face distal to its linker-binding site. Our findings provide new molecular insights on recognition of the canonical nucleosome by a chromatin remodeler and have implications for ATP-driven mechanisms of histone eviction and deposition.

Indexed as

Chromatin Assembly and DisassemblyAdenosine TriphosphatasesChromatinDNAHistonesNucleosomesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesChromatinDNAHistonesNucleosomesSaccharomyces cerevisiae ProteinsSwr1 protein, S cerevisiaebiochemistrychromatin remodelerchromosomesgenesH2A.ZnucleosomeS. cerevisiae

Identifiers

PMID26116819
PMCPMC4508883

What OpenQuestion holds

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Registered trials

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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.