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8Q16

CryoEM structure of rice nucleosome containing a H4 variant chimera

これはPDB形式変換不可エントリーです。
8Q16 の概要
エントリーDOI10.2210/pdb8q16/pdb
関連するPDBエントリー8Q15
EMDBエントリー18060 18061
分子名称Histone H2A.2, Histone H2B.4, Histone H3.2, ... (6 entities in total)
機能のキーワードhistone, nucleosome core particle, rice nucleosome, chromatin, dna binding protein
由来する生物種Oryza
詳細
タンパク質・核酸の鎖数10
化学式量合計205512.26
構造登録者
主引用文献Gandhivel, V.H.,Sotelo-Parrilla, P.,Raju, S.,Jha, S.,Gireesh, A.,Harshith, C.Y.,Gut, F.,Vinothkumar, K.R.,Berger, F.,Jeyaprakash, A.A.,Shivaprasad, P.V.
An Oryza-specific histone H4 variant predisposes H4 lysine 5 acetylation to modulate salt stress responses.
Nat.Plants, 11:790-807, 2025
Cited by
PubMed Abstract: Paralogous variants of canonical histones guide accessibility to DNA and function as additional layers of genome regulation. Across eukaryotes, the mechanism of action and functional significance of several variants of core histones are well known except those of histone H4. Here we show that a variant of H4 (H4.V) expressing tissue-specifically among Oryza members mediated specific epigenetic changes contributing to salt tolerance. H4.V was incorporated into specific heterochromatic sites, where it blocked the deposition of active histone marks. Stress-dependent redistribution of H4.V enabled the incorporation of acetylated H4 lysine 5 (H4K5ac) in the gene bodies. The misexpression of H4.V led to defects in reproductive development and in mounting salt stress responses. H4.V formed homotypic nucleosomes and mediated these alterations by conferring distinct molecular properties to the nucleosomes, as seen with cryo electron microscopy structures and biochemical assays. These results reveal not only an H4 variant among plants but also a chromatin regulation that might have contributed to the adaptation of semi-aquatic Oryza members.
PubMed: 40200022
DOI: 10.1038/s41477-025-01974-2
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.6 Å)
構造検証レポート
Validation report summary of 8q16
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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