Background：

Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3’ to 5’) activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction， tumor suppressor mediated growth arrest and replicative senescence， apoptosis， and DNA repair. The NuA4 complex ATPase and helicase activities seem to be， at least in part， contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct