title: PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase.
abstract: Poly(ADP-ribosylation) is a post-translational modification of nuclear proteins in response to DNA damage that activates the base excision repair machinery. Poly(ADP-ribose) polymerase which we will now call PARP-1, has been the only known enzyme of this type for over 30 years. Here, we describe a cDNA encoding a 62-kDa protein that shares considerable homology with the catalytic domain of PARP-1 and also contains a basic DNA-binding domain. We propose to call this enzyme poly(ADP-ribose) polymerase 2 (PARP-2). The PARP-2 gene maps to chromosome 14C1 and 14q11.2 in mouse and human, respectively. Purified recombinant mouse PARP-2 is a damaged DNA-binding protein in vitro and catalyzes the formation of poly(ADP-ribose) polymers in a DNA-dependent manner. PARP-2 displays automodification properties similar to PARP-1. The protein is localized in the nucleus in vivo and may account for the residual poly(ADP-ribose) synthesis observed in PARP-1-deficient cells, treated with alkylating agents or hydrogen peroxide.
authors.affiliation: UPR 9003 du CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, F-67400 Illkirch, France.
authors.forename: J C
authors.initials: JC
authors.lastname: Amé
authors.forename: V
authors.initials: V
authors.lastname: Rolli
authors.forename: V
authors.initials: V
authors.lastname: Schreiber
authors.forename: C
authors.initials: C
authors.lastname: Niedergang
authors.forename: F
authors.initials: F
authors.lastname: Apiou
authors.forename: P
authors.initials: P
authors.lastname: Decker
authors.forename: S
authors.initials: S
authors.lastname: Muller
authors.forename: T
authors.initials: T
authors.lastname: Höger
authors.forename: J
authors.initials: J
authors.lastname: Ménissier-de Murcia
authors.forename: G
authors.initials: G
authors.lastname: de Murcia
mesh_terms: D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D002874:Chromosome Mapping; D002883:Chromosomes, Human, Pair 14 / Q000235:genetics; D003001:Cloning, Molecular; D004249:DNA Damage / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics; D004789:Enzyme Activation / Q000235:genetics; D006801:Humans; D017404:In Situ Hybridization, Fluorescence; D008214:Lymphocytes / Q000201:enzymology; D051379:Mice; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry / Q000235:genetics*; D012333:RNA, Messenger / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics; D016415:Sequence Alignment
chemical_list: D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D012333:RNA, Messenger; D011994:Recombinant Proteins; D011065:Poly(ADP-ribose) Polymerases