InterPro domain: IPR008288

Poly(ADP-ribose) synthase and poly(ADP-ribose) polymerase (PARP, also known as ADPRT) catalyse the DNA-dependent covalent attachment of ADP-ribose to various nuclear proteins [ 1 ]. They are used by the eukaryotic cell to cope with numerous environmental and endogenous genotoxic agents that cause DNA strand breaks. PARP plays a role in many cellular processes, including DNA repair, recombination, cell proliferation and death, as well as genomic stability [ 2 ]. The DNA-binding region of the protein contains a pair of zinc finger domains, which have been shown to bind DNA in a zinc-dependent manner [ 3 ]. PARP also contains a BRCT domain involved in cell cycle checkpoint functions responsive to DNA damage [ 4 ], a catalyic domain and a regulatory domain.

1. ADP-ribosylation of proteins. Enzymology and biological significance. Biochim. Biophys. Acta 37, 1-237
2. Poly(ADP-ribose) polymerase: a guardian angel protecting the genome and suppressing tumorigenesis. Eur. J. Biochem. 1552, 27-37
3. Poly(ADP-ribose) polymerase is a zinc metalloenzyme. null 142, 503-9
4. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J. 11, 68-76