Evidence map›Paper›PMID 24507717›Full record

ArticleMolecular cell2014

The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer.

Jingjun Hong, Hanqiao Feng, Feng Wang, Anand Ranjan, Jianhong Chen, Jiansheng Jiang, Rodolfo Ghirlando, T Sam Xiao, Carl Wu, Yawen Bai

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

54 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Specialized RSC: Substrate Specificities for a Conserved Chromatin Remodeler.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020
    Article
  18. eLife · 2020
    Article
  19. Review
  20. Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

10 authors at 4 institutions in 1 country.

Jingjun HongLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Hanqiao FengLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Feng WangLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Anand RanjanLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Jianhong ChenLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Jiansheng JiangLaboratory of Immunology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.
Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892, USA.
T Sam XiaoLaboratory of Immunology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.
Carl WuLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA; Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USA.
Yawen BaiLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA. Electronic address: yawen@helix.nih.gov.
National Cancer Institute · USNational Institute of Allergy and Infectious Diseases · USJanelia Research Campus · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Nucleosome DynamicsZIABC010808 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BAI, YAWEN · 2009 to 2025
$26.5M
Structural Studies of Pattern Recognition ReceptorsZIAAI000960 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI XIAO, TSAN · 2009 to 2014
$6.1M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Nucleosome DynamicsZ01BC010808 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BAI, YAWEN · 2007 to 2008
$329k
Howard Hughes Medical InstituteIntramural NIH HHS Z01 BC010808NCI NIH HHS Y1-CO-1020NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Histone variant H2A.Z-containing nucleosomes exist at most eukaryotic promoters and play important roles in gene transcription and genome stability. The multisubunit nucleosome-remodeling enzyme complex SWR1, conserved from yeast to mammals, catalyzes the ATP-dependent replacement of histone H2A in canonical nucleosomes with H2A.Z. How SWR1 catalyzes the replacement reaction is largely unknown. Here, we determined the crystal structure of the N-terminal region (599-627) of the catalytic subunit Swr1, termed Swr1-Z domain, in complex with the H2A.Z-H2B dimer at 1.78 Å resolution. The Swr1-Z domain forms a 310 helix and an irregular chain. A conserved LxxLF motif in the Swr1-Z 310 helix specifically recognizes the αC helix of H2A.Z. Our results show that the Swr1-Z domain can deliver the H2A.Z-H2B dimer to the DNA-(H3-H4)2 tetrasome to form the nucleosome by a histone chaperone mechanism.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceChromatin Assembly and DisassemblyCloning, MolecularCrystallography, X-RayDimerizationHistonesModels, MolecularMolecular Sequence DataProtein Structure, TertiaryProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsX-Ray DiffractionAdenosine TriphosphatasesHistonesProtein SubunitsSaccharomyces cerevisiae ProteinsSwr1 protein, S cerevisiae

Identifiers

PMID24507717
PMCPMC3940207
OpenAlexW2030093830

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.