Molecular and structural basis of the chromatin remodeling activity by Arabidopsis DDM1.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
11 Jul 2024
11 Jul 2024
Historique:
received:
10
07
2023
accepted:
05
06
2024
medline:
12
7
2024
pubmed:
12
7
2024
entrez:
11
7
2024
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 38992002
doi: 10.1038/s41467-024-49465-w
pii: 10.1038/s41467-024-49465-w
doi:
Substances chimiques
Arabidopsis Proteins
0
Nucleosomes
0
Histones
0
DDM1 protein, Arabidopsis
0
Transcription Factors
0
DNA-Binding Proteins
0
DNA, Plant
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
5187Subventions
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : JP22H05172
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : JP22H05178
Organisme : MEXT | JST | Precursory Research for Embryonic Science and Technology (PRESTO)
ID : JPMJPR20K3
Informations de copyright
© 2024. The Author(s).
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