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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 Lys20 acetylation (H4K20ac) is catalyzed by p300/CBP. Distinct from repressive H4K20me marks, H4K20ac correlates with transcriptional activation at promoters and enhancers. It participates in cell cycle progression and DNA damage signal transduction; HDAC inhibitor treatment significantly elevates global H4K20ac abundance.
