biostudies-literatureBennett GNIGMS NIH HHS38-45https://www.ebi.ac.uk/biostudies/studies/S-EPMC4425604biostudies-literatureUnknown30The DNA damage response to double-strand breaks (DSBs) is critical for cellular viability. Recent work has shown that a host of chromatin regulators are recruited to a DSB, and that they are important for the DNA damage response. However, the functional relationships between different chromatin regulators at DSBs remain unclear. Here we describe a conserved functional interaction among the chromatin remodeling enzyme, SWI/SNF, the NuA4 and Gcn5 histone acetyltransferases, and phosphorylation of histone H2A.X (?H2AX). Specifically, we find that the NuA4 and Gcn5 enzymes are both required for the robust recruitment of SWI/SNF to a DSB, which in turn promotes the phosphorylation of H2A.X.DNA repairSWI/SNF recruitment to a DNA double-strand break by the NuA4 and Gcn5 histone acetyltransferases.PMC4425604R01 GM054096GM54096Bennett GPeterson CLfalseSWI/SNF recruitment to a DNA double-strand break by the NuA4 and Gcn5 histone acetyltransferases.The DNA damage response to double-strand breaks (DSBs) is critical for cellular viability. Recent work has shown that a host of chromatin regulators are recruited to a DSB, and that they are important for the DNA damage response. However, the functional relationships between different chromatin regulators at DSBs remain unclear. Here we describe a conserved functional interaction among the chromatin remodeling enzyme, SWI/SNF, the NuA4 and Gcn5 histone acetyltransferases, and phosphorylation of histone H2A.X (?H2AX). Specifically, we find that the NuA4 and Gcn5 enzymes are both required for the robust recruitment of SWI/SNF to a DSB, which in turn promotes the phosphorylation of H2A.X.2015-01-01T00:00:00Z2015 Jun2020-10-29T11:41:49Z2019-03-27T01:51:17ZS-EPMC44256042586982310.1016/j.dnarep.2015.03.006