Structure-function relationship of ASH1L and histone H3K36 and H3K4 methylation.

ABSTRACT: The histone H3K36-specific methyltransferase ASH1L plays a critical role in development and is frequently dysregulated in human diseases, particularly cancer. Here, we report on the biological functions of the C-terminal region of ASH1L encompassing a bromodomain (ASH1L_BD), a plant homeodomain (ASH1L_PHD) finger, and a bromo-adjacent homology (ASH1L_BAH) domain, structurally characterize these domains, describe their mechanisms of action, and explore functional crosstalk between them. We find that ASH1L_PHD recognizes H3K4me2/3, whereas the neighboring ASH1L_BD and ASH1L_BAH have DNA binding activities. The DNA binding function of ASH1L_BAH is a driving force for the association of ASH1L with the linker DNA in the nucle

SUBMITTER: Vann KR 

PROVIDER: S-EPMC11883000 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature