Widespread association of Polycomb complex-deposited histone H2A monoubiquitylation with enhancers and neuronal gene regulation.

ABSTRACT: Disruption of histone H2A monoubiquitylation (H2AK119ub) causes neurodevelopmental disorders through poorly understood mechanisms. Polycomb complex-deposited H2AK119ub and trimethylation of histone H3 at lysine 27 (H3K27me3) can cooperatively maintain gene repression. However, the extent to which H2AK119ub functions independently of H3K27me3 to repress or potentiate gene expression, and the evolutionary conservation of these roles, remains unclear. Here, we address the interplay among Polycomb-deposited marks and chromatin states in Caenorhabditis elegans embryos. We find that H2AK119ub distribution is distinct from and largely dispensable for H3K27me3 patterns. Unexpectedly, H2AK119ub is enriched at predicted enhancers with developmentally dynamic changes in accessibility, includin

SUBMITTER: MacGillivray K 

PROVIDER: S-EPMC12652333 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature