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Background The NuA4 histone acetyltransferase is a highly conserved multisubunit complex responsible for acetylation of nucleosomal histone H4 and H2A. Mutations in different NuA4 subunits create cell cycle arrest or delay in G2/M. The NuA4 complex is important for gene expression but also the efficient repair of DNA double strand breaks (DSBs) in vivo. NuA4 is rapidly recruited to chromatin surrounding a DSB in vivo at the same time histone H2A (X) is phosphorylated in the neighboring region (g-H2AX). While we have shown that NuA4 can interact with phosphorylated H2A(X), we speculated that another interaction was required for the initial recruitment of NuA4 at the break. Based on the presence of an ATM-related factor within NuA4, the subunitTra1 (TRRAP), it was tempting to postulate that DSB sensing factors known to recruit ATM family PIKK factors could be responsible for NuA4 recruitment.

Phospho-dependent recruitment of NuA4 by MRX at DNA breaks regulates RPA dynamics during resection