6JMA

cryo-EM structure of DOT1L bound to H2B ubiquitinated nucleosome

6JMA の概要

• エントリーDOI: 10.2210/pdb6jma/pdb
• EMDBエントリー: 9843 9844
• 分子名称: DNA I&J, Histone H3.2, Histone H4, ... (8 entities in total)
• 機能のキーワード: histone, nucleosome, methylation, gene regulation
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 206478.26

構造登録者

Jang, S.,Song, J.J. (登録日: 2019-03-07, 公開日: 2019-05-15, 最終更新日: 2024-03-27)

主引用文献

Jang, S.,Kang, C.,Yang, H.S.,Jung, T.,Hebert, H.,Chung, K.Y.,Kim, S.J.,Hohng, S.,Song, J.J.
Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase.
Genes Dev., 33:620-625, 2019

PubMed Abstract: DOT1L is a histone H3 Lys79 methyltransferase whose activity is stimulated by histone H2B Lys120 ubiquitination, suggesting cross-talk between histone H3 methylation and H2B ubiquitination. Here, we present cryo-EM structures of DOT1L complexes with unmodified or H2B ubiquitinated nucleosomes, showing that DOT1L recognizes H2B ubiquitin and the H2A/H2B acidic patch through a C-terminal hydrophobic helix and an arginine anchor in DOT1L, respectively. Furthermore, the structures combined with single-molecule FRET experiments show that H2B ubiquitination enhances a noncatalytic function of the DOT1L-destabilizing nucleosome. These results establish the molecular basis of the cross-talk between H2B ubiquitination and H3 Lys79 methylation as well as nucleosome destabilization by DOT1L.

PubMed: 30923167
DOI: 10.1101/gad.323790.118

実験手法

ELECTRON MICROSCOPY (6.8 Å)