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Background:Histone H4 assembles with H3 to form H3-H4 tetramer, the core scaffold of nucleosome. Reversible lysine acetylation on H4 N-terminal tail and core domain is regulated by HAT and HDAC. Acetylation eliminates positive charge of histone tails, loosens chromatin and recruits bromodomain co-activators. Different acetylated lysine sites on H4 perform unique functions in gene transcription, DNA replication, DNA damage repair and epigenetic silencing regulation. H4 Lys12 acetylation (H4K12ac) is a classic marker of newly synthesized histones following DNA replication, catalyzed by HAT1 complex. It maintains chromatin accessibility for transcription machinery and facilitates post-replication chromatin maturation. H4K12ac also accumulates at damage foci to coordinate homologous recombination repair.
