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Mol Cell ; 83(17): 3080-3094.e14, 2023 09 07.
Artigo em Inglês | MEDLINE | ID: mdl-37633270

RESUMO

Histone H2B monoubiquitylation plays essential roles in chromatin-based transcriptional processes. A RING-type E3 ligase (yeast Bre1 or human RNF20/RNF40) and an E2 ubiquitin-conjugating enzyme (yeast Rad6 or human hRAD6A), together, precisely deposit ubiquitin on H2B K123 in yeast or K120 in humans. Here, we developed a chemical trapping strategy and successfully captured the transient structures of Bre1- or RNF20/RNF40-mediated ubiquitin transfer from Rad6 or hRAD6A to nucleosomal H2B. Our structures show that Bre1 and RNF40 directly bind nucleosomal DNA, exhibiting a conserved E3/E2/nucleosome interaction pattern from yeast to humans for H2B monoubiquitylation. We also find an uncanonical non-hydrophobic contact in the Bre1 RING-Rad6 interface, which positions Rad6 directly above the target H2B lysine residue. Our study provides mechanistic insights into the site-specific monoubiquitylation of H2B, reveals a critical role of nucleosomal DNA in mediating E3 ligase recognition, and provides a framework for understanding the cancer-driving mutations of RNF20/RNF40.


Assuntos
Nucleossomos , Proteínas de Saccharomyces cerevisiae , Humanos , Nucleossomos/genética , Histonas/genética , Saccharomyces cerevisiae/genética , Ubiquitina , Ubiquitina-Proteína Ligases/genética , Proteínas de Saccharomyces cerevisiae/genética
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