PROSITE documentation PDOC00360Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature and profile
Poly(ADP-ribose) polymerase (EC 2.4.2.30) (PARP) [1,2] is a eukaryotic enzyme that catalyzes the covalent attachment of ADP-ribose units from NAD(+) to various nuclear acceptor proteins. 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 tumor transformation as well as in the regulation of the molecular events involved in the recovery of the cell from DNA damage.
Structurally, PARP, about 1000 amino-acids residues long, 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 zinc finger domains which have been shown to bind DNA in a zinc-dependent manner. The zinc finger domains of PARP seem to bind specifically to single-stranded DNA.
DNA ligase III [3] contains, in its N-terminal section, a single copy of a zinc finger highly similar to those of PARP.
Expert(s) to contact by email: Last update:September 2022 / Text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Althaus F.R. Richter C.R. |
| Title | ADP-ribosylation of proteins. Enzymology and biological significance. | |
| Source | Mol. Biol. Biochem. Biophys. 37:1-237(1987). | |
| PubMed ID | 3118181 |
| 2 | Authors | de Murcia G. Menissier de Murcia J. |
| Source | Trends Biochem. Sci. 19:172-176(1994). |
| 3 | Authors | Wei Y.-F. Robins P. Carter K. Caldecott K. Pappin D.J.C. Yu G.-L. Wang R.-P. Shell B.K. Nash R.A. Schar P. Barnes D.E. Haseltine W.A. Lindahl T. |
| Title | 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. | |
| Source | Mol. Cell. Biol. 15:3206-3216(1995). | |
| PubMed ID | 7760816 |
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