InterPro domain: IPR036957

This entry represents the PARP (poly ADP-ribose polymerase) type zinc finger domain superfamily.

PARP, also known as NAD(+) ADP-ribosyltransferase ( 2.4.2.30 ), is a eukaryotic enzyme that catalyses the covalent attachment of ADP-ribose units from NAD(+) to various nuclear acceptor proteins [ 1 , 2 ]. This post-translational modification of nuclear proteins is dependent on DNA. It appears to be involved in the regulation of various important cellular processes such as differentiation, proliferation and tumour transformation as well as in the regulation of the molecular events involved in the recovery of the cell from DNA damage. Structurally, NAD(+) ADP-ribosyltransferase consists of three distinct domains: an N-terminal zinc-dependent DNA-binding domain, a central automodification domain and a C-terminal NAD-binding domain. The DNA-binding region contains a pair of PARP-type zinc finger domains which have been shown to bind DNA in a zinc-dependent manner. The PARP-type zinc finger domains seem to bind specifically to single-stranded DNA and to act as a DNA nick sensor. DNA ligase III [ 3 ] contains, in its N-terminal section, a single copy of a zinc finger highly similar to those of PARP.

1. ADP-ribosylation of proteins. Enzymology and biological significance. Mol. Cell. Biol. 37, 1-237
2. Poly(ADP-ribose) polymerase: a molecular nick-sensor. IUBMB Life 19, 172-6
3. Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Trends Biochem. Sci. 15, 3206-16