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Background：
Histone H2A.X is an essential H2A variant primarily responsible for genome stability and cellular DNA damage response. Upon DNA double-strand breaks, H2A.X undergoes C-terminal phosphorylation to form γH2A.X, which initiates the recruitment of multiple repair factors and activates DNA damage checkpoints. Dynamic lysine acetylation on the N-terminal tail of H2A.X cooperates with phosphorylation to regulate chromatin remodeling, DNA repair efficiency and basal transcription.H2A.X Lys5 acetylation (H2A.X K5ac) is mainly catalyzed by the TIP60 complex at DNA damage sites. This modification recruits DNA-PK and MRN repair complexes, promotes γH2A.X formation, and supports both homologous recombination and non-homologous end joining. Loss of H2A.X K5ac leads to defective DNA repair, genome instability and increased cellular radiosensitivity.
