MOZ/MORF

MOZ (KAT6A) and MORF (KAT6B) are paralogous members of the MYST family of lysine acetyltransferases that function in multisubunit chromatin-regulatory complexes and catalyze histone H3 acetylation to promote transcriptionally active chromatin states[1][2]. Mechanistically, MOZ/MORF complexes interact with BRPF and ING proteins, integrate histone-reader functions with catalytic activity, and regulate chromatin-dependent gene expression programs involved in development, stem-cell maintenance, and hematopoiesis[1][3][4]. Recent structural and genomic studies further demonstrated that MOZ and MORF recognize unmethylated CpG-rich promoter regions through N-terminal winged-helix domains, facilitating promoter targeting, H3K23 acetylation, and transcriptional activation[5]. These chromatin-regulatory activities are closely linked to biological processes including embryogenesis, skeletogenesis, cellular differentiation, and maintenance of hematopoietic stem-cell function[3][4][5]. Disease relevance is supported by recurrent chromosomal rearrangements involving KAT6A or KAT6B in acute myeloid leukemia and related hematologic malignancies, as well as developmental disorders associated with germline variants in either gene[2][4]. Compared with related MYST family acetyltransferases, MOZ and MORF share high sequence homology and similar domain organization, yet they function as distinct catalytic subunits within mutually exclusive complexes and can display context-dependent biological specialization[2][6]. For experimental applications, MOZ/MORF-containing complexes provide a tractable model for investigating epigenetic regulation, chromatin targeting mechanisms, and acetyltransferase-dependent transcriptional control in development and disease[1][3][5].