Histone H3 Orchestrates the Ubiquitination of Nucleosomal H2A by BRCA1/BARD1-UbcH5c Complex.

This article discusses the role of the BRCA1/BARD1-UbcH5c complex in the ubiquitination of the C-terminal H2A, which is important for repairing double-stranded DNA breaks. The study used molecular dynamics simulations to model the complex and found that the ubiquitin protein (Ub) covalently bonds to the active site of E2, affecting the flexibility of the E3-E2 complex. The study also suggests that histone H3 may play a role in determining the preferred orientation of E2-Ub with respect to the H2A C-terminal lysines. However, it should be noted that this preprint has not been peer-reviewed. [Extracted from the article]