8GUK

Human nucleosome core particle (free form)

8GUK の概要

• エントリーDOI: 10.2210/pdb8guk/pdb
• 関連するPDBエントリー: 8GUI 8GUJ
• EMDBエントリー: 34274 34275
• 分子名称: Histone H3.1, Histone H4, Histone H2A type 1, ... (6 entities in total)
• 機能のキーワード: transcription, ubiquitin ligase, cancer, chromatin, gene regulation, gene regulation-dna complex, gene regulation/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 200566.31

構造登録者

Onishi, S.,Sato, K.,Nishizawa, T.,Nureki, O.,Ogata, K.,Sengoku, T. (登録日: 2022-09-12, 公開日: 2023-09-20, 最終更新日: 2025-07-02)

主引用文献

Onishi, S.,Uchiyama, K.,Sato, K.,Okada, C.,Kobayashi, S.,Hamada, K.,Nishizawa, T.,Nureki, O.,Ogata, K.,Sengoku, T.
Structure of the human Bre1 complex bound to the nucleosome.
Nat Commun, 15:2580-2580, 2024

PubMed Abstract: Histone H2B monoubiquitination (at Lys120 in humans) regulates transcription elongation and DNA repair. In humans, H2B monoubiquitination is catalyzed by the heterodimeric Bre1 complex composed of Bre1A/RNF20 and Bre1B/RNF40. The Bre1 proteins generally function as tumor suppressors, while in certain cancers, they facilitate cancer cell proliferation. To obtain structural insights of H2BK120 ubiquitination and its regulation, we report the cryo-electron microscopy structure of the human Bre1 complex bound to the nucleosome. The two RING domains of Bre1A and Bre1B recognize the acidic patch and the nucleosomal DNA phosphates around SHL 6.0-6.5, which are ideally located to recruit the E2 enzyme and ubiquitin for H2BK120-specific ubiquitination. Mutational experiments suggest that the two RING domains bind in two orientations and that ubiquitination occurs when Bre1A binds to the acidic patch. Our results provide insights into the H2BK120-specific ubiquitination by the Bre1 proteins and suggest that H2B monoubiquitination can be regulated by nuclesomal DNA flexibility.

PubMed: 38519511
DOI: 10.1038/s41467-024-46910-8

実験手法

ELECTRON MICROSCOPY (2.51 Å)