Evidence map›Paper›PMID 38992002›Full record

ArticleNature communications2024

Molecular and structural basis of the chromatin remodeling activity by Arabidopsis DDM1.

Akihisa Osakabe, Yoshimasa Takizawa, Naoki Horikoshi, Suguru Hatazawa, Lumi Negishi, Shoko Sato, Frédéric Berger, Tetsuji Kakutani, Hitoshi Kurumizaka

Abstract read
In one paragraph

Article in Nature communications, 2024. 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
–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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. CDCA7 facilitates MET1-mediated CG DNA methylation maintenance in centromeric heterochromatin via linker histone H1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. DDM1 Maintains Heterochromatin by Regulating Histone Variants.International journal of molecular sciences · 2025
    Review
  15. Review
  16. Article
  17. Mutation ofPlants (Basel, Switzerland) · 2025
    Article
  18. 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

9 authors.

Akihisa Osakabe *Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan. akihisa-osakabe@g.ecc.u-tokyo.ac.jp.ORCID 0000-0002-2526-3398
Yoshimasa Takizawa *Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-6265-4830
Naoki HorikoshiLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.
Suguru HatazawaLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-5678-4049
Lumi NegishiLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-7297-0634
Shoko SatoLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-9926-2961
Frédéric BergerGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna Biocenter (VBC), Vienna, Austria.ORCID 0000-0002-3609-8260
Tetsuji KakutaniDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan. tkak@bs.s.u-tokyo.ac.jp.ORCID 0000-0002-6137-4474
Hitoshi KurumizakaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan. kurumizaka@iqb.u-tokyo.ac.jp.ORCID 0000-0001-7412-3722

Funding

Austrian Science Fund FWF P 32054Austrian Science Fund FWF P 33380MEXT | Japan Society for the Promotion of Science (JSPS) JP22H05172MEXT | Japan Society for the Promotion of Science (JSPS) JP22H05178MEXT | JST | Precursory Research for Embryonic Science and Technology (PRESTO) JPMJPR20K3
6 · The paper itself

Abstract

The histone H2A variant H2A.W occupies transposons and thus prevents access to them in Arabidopsis thaliana. H2A.W is deposited by the chromatin remodeler DDM1, which also promotes the accessibility of chromatin writers to heterochromatin by an unknown mechanism. To shed light on this question, we solve the cryo-EM structures of nucleosomes containing H2A and H2A.W, and the DDM1-H2A.W nucleosome complex. These structures show that the DNA end flexibility of the H2A nucleosome is higher than that of the H2A.W nucleosome. In the DDM1-H2A.W nucleosome complex, DDM1 binds to the N-terminal tail of H4 and the nucleosomal DNA and increases the DNA end flexibility of H2A.W nucleosomes. Based on these biochemical and structural results, we propose that DDM1 counters the low accessibility caused by nucleosomes containing H2A.W to enable the maintenance of repressive epigenetic marks on transposons and prevent their activity.

Indexed as

ArabidopsisArabidopsis ProteinsChromatin Assembly and DisassemblyCryoelectron MicroscopyHistonesNucleosomesDNA-Binding ProteinsDNA, PlantModels, MolecularProtein BindingTranscription FactorsArabidopsis ProteinsDDM1 protein, ArabidopsisDNA-Binding ProteinsDNA, PlantHistonesNucleosomesTranscription Factors

Identifiers

PMID38992002
PMCPMC11239853

What Socratic holds

Textmetadata
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 Socratic graph.