DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding. ATP + H2O = ADP + H(+) + phosphate Localizes at sites of DNA damage. The macro domain mediates non-covalent poly(ADP-ribose)-binding and recruitment to DNA damage sites (By similarity). Mediates auto-inhibition of ATPase activity by interacting with the N-terminal ATPase module, encompassing the helicase ATP-binding domain and helicase C-terminal domain (By similarity). PARP1 activation upon DNA damage and poly(ADP-ribose)-binding release the auto-inhibition by the macro domain and trigger ATPase activity (By similarity). Belongs to the SNF2/RAD54 helicase family.