Structural insights into the Bre1-Lge1 and RNF20/RNF40-WAC interactions critical for H2B ubiquitination.

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 interfac

SUBMITTER: Shi M 

PROVIDER: S-EPMC12802937 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature