Histone H3K23-specific acetylation by MORF is coupled to H3K14 acylation.

ABSTRACT: Acetylation of histone H3K23 has emerged as an essential posttranslational modification associated with cancer and learning and memory impairment, yet our understanding of this epigenetic mark remains insufficient. Here, we identify the native MORF complex as a histone H3K23-specific acetyltransferase and elucidate its mechanism of action. The acetyltransferase function of the catalytic MORF subunit is positively regulated by the DPF domain of MORF (MORF_DPF). The crystal structure of MORF_DPF in complex with crotonylated H3K14 peptide provides mechanistic insight into selectivity of this epigenetic reader and its ability to recognize both histone and DNA. ChIP data reveal the role of MORF_DPF in MORF-dependent H3K23 acetylation of target genes. Mass spectrome

SUBMITTER: Klein BJ 

PROVIDER: S-EPMC6797804 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature