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Background:Histone H3 forms tetramers with H4 to build chromatin skeleton. Its N-terminal tail and globular core lysine residues undergo reversible acetylation dynamically regulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs). Acetylation neutralizes positive charge of lysine residues, weakens histone-DNA binding to relax compact chromatin, and provides binding epitopes for bromodomain-containing transcriptional co-activators. Different acetylation sites on H3 separately participate in transcription initiation, gene elongation, DNA damage repair, cell cycle control and genome stability maintenance. H3 Lys79 (H3K79) locates on the surface of H3 globular core domain, distinct from common N-tail modification sites. H3K79 acetylation (H3K79ac) is mainly catalyzed by p300/CBP and KAT2A, while sirtuin family HDACs mediate its deacetylation. This modification is a marker of transcriptionally active chromatin, enriched at coding regions of highly expressed genes to facilitate RNA polymerase II elongation. H3K79ac cooperates with H3K79 methylation to coordinate DNA double-strand break repair and resolve transcription-replication conflicts; abnormal H3K79ac level is closely associated with tumor proliferation and epithelial-mesenchymal transition.
