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 () and Hitoshi Kurumizaka ()
Additional contact information
Akihisa Osakabe: The University of Tokyo
Yoshimasa Takizawa: The University of Tokyo
Naoki Horikoshi: The University of Tokyo
Suguru Hatazawa: The University of Tokyo
Lumi Negishi: The University of Tokyo
Shoko Sato: The University of Tokyo
Frédéric Berger: Vienna Biocenter (VBC)
Tetsuji Kakutani: The University of Tokyo
Hitoshi Kurumizaka: The University of Tokyo

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: 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.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-49465-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49465-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-49465-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().