Fig. 2: Mapping the SPINDOC and PARP1-interaction domain.

a Domain structure and deletion/mutation constructs for PARP1. Up panel: The major domains and active catalytic sites of PARP1 are marked, DBD: DNA-binding domain, including 1–373aa, ZF1: zinc finger 1, ZF2: zinc finger 2, ZF3: zinc finger 3, NLS: nuclear-localization signal, D214N: caspase-cleavage site, BRCT: BRCA1 C-terminal, AD: automodification domain, CD: catalytic domains, including WGR domain and PARP1-signature domain. b HEK293T cells were transfected with the listed constructs and subjected to GFP IP after 48 h, and analyzed by Western blot using the indicated antibodies. The results were repeated three times independent experiments, shown as representative blots. c Domain structure and deletion constructs for SPINDOC. SPINDOC251–293aa is SPIN1-binding motif. d HEK293T cells were transfected with the listed constructs and subjected to GFP IP after 48 h, and analyzed by Western blot using the indicated antibodies. The results were shown as representative blots from three times independent experiments.