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9K43

Cryo-EM structure of Arabidopsis thaliana H2A.Z-nucleosome with 147bp Widom 601 DNA (C2 symmetry)

Summary for 9K43
Entry DOI10.2210/pdb9k43/pdb
EMDB information62041 62042
DescriptorHistone H3.1, Histone H4, Probable histone H2A variant 3, ... (6 entities in total)
Functional Keywordsnucleosome, histone, h2a.z, arabidopsis, nuclear protein/dna, nuclear protein-dna complex
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains10
Total formula weight205706.67
Authors
Wang, Y.,Dong, A. (deposition date: 2024-10-21, release date: 2025-05-14, Last modification date: 2025-05-28)
Primary citationWang, Y.,Wu, J.,Yang, S.,Li, X.,Wang, J.,Lv, Q.,Zhu, X.,Lu, G.,Zhang, J.,Shen, W.H.,Liu, B.,Lin, J.,Dong, A.
Structural and functional interrelationships of histone H2A with its variants H2A.Z and H2A.W in Arabidopsis.
Structure, 2025
Cited by
PubMed Abstract: Multiple histone H2A variants are known in eukaryotes. However, the functional relationship between H2A and its variants in plants remains largely obscure. Using CRISPR-Cas9 editing, we generated a mutant lacking four H2A isoforms in Arabidopsis and analyzed the functional and structural relationships between H2A, H2A.Z, and H2A.W. RNA sequencing and phenotype analyses revealed mild changes in gene transcription and plant development in mutants lacking H2A, H2A.Z, or H2A.W compared with the wild-type plants. Chromatin immunoprecipitation sequencing analysis showed that H2A can substitute for both H2A.Z and H2A.W across the genome, including in euchromatin and heterochromatin regions. However, H2A.Z replaced both H2A and H2A.W primarily within the euchromatin regions. By using DNA and histones from Arabidopsis, we constructed nucleosomes containing H2A, H2A.Z, or H2A.W and resolved their cryogenic electron microscopy (cryo-EM) structures at near-atomic resolution. Collectively, the results reveal the structural similarity and functional redundancy of H2A and its variants in Arabidopsis.
PubMed: 40359943
DOI: 10.1016/j.str.2025.04.015
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.87 Å)
Structure validation

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