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Background：
Canonical histone H2B heterodimerizes with H2A to assemble the core nucleosome particle. Reversible lysine acetylation on the flexible N-terminal tail of H2B is a classic marker of transcription-permissive chromatin. Acetylation neutralizes positive charges of histone tails, weakens histone-DNA interaction and creates binding sites for bromodomain-containing co-activators. Different lysine sites on H2B tail carry distinct functions in transcription initiation, elongation and post-damage chromatin recovery. 2B Lys5 acetylation (H2B K5ac) is catalyzed by p300/CBP and accumulates at active gene promoters and enhancers. Multi-site acetylation of H2B N-tail synergistically relaxes chromatin and recruits transcriptional co-activators. H2B K5ac co-localizes with active enhancer marker H3K27ac and dynamically changes during cell cycle progression and cell differentiation.
