9M3I

Crystal structure of the Bre1-Lge1 complex

9M3I の概要

• エントリーDOI: 10.2210/pdb9m3i/pdb
• 分子名称: E3 ubiquitin-protein ligase BRE1, Transcriptional regulatory protein LGE1 (3 entities in total)
• 機能のキーワード: ubiquitin ligase, gene regulation
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 117601.05

構造登録者

Zhang, H.,Xiang, S. (登録日: 2025-03-02, 公開日: 2026-01-14, 最終更新日: 2026-03-04)

主引用文献

Shi, M.,Wang, X.,Zhang, H.,Wen, Y.,Liu, Q.,Chen, P.,Chen, X.,Xiang, S.
Structural insights into the Bre1-Lge1 and RNF20/RNF40-WAC interactions critical for H2B ubiquitination.
Nucleic Acids Res., 54:-, 2026

PubMed Abstract: The mono-ubiquitination of the histone protein H2B (H2BUb1) has important functions in transcription, DNA repair, and other chromatin-related processes. The reaction is catalyzed by Bre1 and the homologous RNF20/RNF40 complex in the budding yeast and human cells, respectively, and is promoted by their respective interaction partners, Lge1 and WAC. The mechanism of the Bre1-Lge1 and RNF20/RNF40-WAC interactions is poorly understood. Here, we present the crystal structure of the Bre1-Lge1 complex and an AlphaFold predicted structure model of the RNF20/RNF40 complex bound with WAC, as well as in vitro and in vivo experiments to assess the interaction mechanism and function. Our study revealed extensive Bre1-Lge1 and RNF20/RNF40-WAC interfaces and a structural homology shared by these interfaces, but completely different sets of key electrostatic interactions at these interfaces that are crucial for the binding and encode the binding specificity. We further found that these interactions play critical roles in the Bre1-catalyzed H2BUb1 reaction and processes it regulates. Our data provide insights into the mechanism of the Bre1-Lge1 and RNF20/RNF40-WAC interactions.

PubMed: 41533567
DOI: 10.1093/nar/gkaf1514

実験手法

X-RAY DIFFRACTION (3.5 Å)