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Background：
Histone H2A.Z is a highly conserved histone variant deposited at nearly all mammalian gene promoters and enhancers by the SWR1 chromatin remodeler complex. It exerts dual regulatory effects on transcription: unmodified H2A.Z tends to form repressive nucleosomes, while N-terminal lysine acetylation converts H2A.Z into an activating epigenetic marker to loosen chromatin and drive gene expression in stem cell maintenance, cell differentiation and signal response. H2A.Z Lys4 acetylation (H2A.Z K4ac) is catalyzed by p300/CBP and TIP60, and frequently coexists with H2A.Z K7ac. K4/K7 diacetylation provides high-affinity binding epitopes for BET family proteins to initiate transcriptional activation. Genome-wide ChIP-seq confirms H2A.Z K4ac marks transcriptionally active promoters and poised enhancers; depletion of this modification suppresses stemness and differentiation gene programs. H2A.Z Lys7 acetylation (H2A.Z K7ac) is the major activating modification on H2A.Z, mainly catalyzed by p300/CBP. It synergizes with H2A.Z K4ac to destabilize promoter nucleosomes and recruit RNA polymerase II. BET bromodomains preferentially bind K4/K7 diacetylated H2A.Z to sustain robust transcription. HDAC inhibitor treatment markedly elevates global H2A.Z K7ac levels.
