PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
| Autor: | Valérie Schreiber, Jean-Christophe Amé, Patrice Decker, V. Rolli, Gilbert de Murcia, Thomas Höger, Josiane Ménissier-de Murcia, Sylviane Muller, Françoise Apiou, Claude Niedergang |
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| Přispěvatelé: | Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS), Immuno-Rhumatologie Moléculaire, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Strasbourg (UNISTRA), Physiopathologie, cibles et thérapies de la polyarthrite rhumatoïde (Li2P), Université Paris 13 (UP13)-Université Sorbonne Paris Cité (USPC)-UFR Santé, Médecine et Biologie Humaine-Institut National de la Santé et de la Recherche Médicale (INSERM), Immunologie et chimie thérapeutiques (ICT), Cancéropôle du Grand Est-Centre National de la Recherche Scientifique (CNRS), Cancérogenèse et mutagenèse moléculaire et structurale (CMMS), Centre National de la Recherche Scientifique (CNRS), Biotechnologie et signalisation cellulaire, Ecole Supérieure de Biotechnologie de Strasbourg, Institut National de la Santé et de la Recherche Médicale (INSERM)-UFR Santé, Médecine et Biologie Humaine-Université Sorbonne Paris Cité (USPC)-Université Paris 13 (UP13) |
| Rok vydání: | 1999 |
| Předmět: |
DNA damage
Poly ADP ribose polymerase Molecular Sequence Data Biology Biochemistry Mice 03 medical and health sciences 0302 clinical medicine Complementary DNA Animals Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Lymphocytes RNA Messenger Cloning Molecular [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] Molecular Biology Poly(ADP-ribose) glycohydrolase In Situ Hybridization Fluorescence ComputingMilieux_MISCELLANEOUS Polymerase 030304 developmental biology Chromosomes Human Pair 14 0303 health sciences PARG Chromosome Mapping Nuclear Proteins 3T3 Cells Cell Biology Base excision repair Molecular biology Recombinant Proteins [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] DNA-Binding Proteins Enzyme Activation 030220 oncology & carcinogenesis biology.protein Poly(ADP-ribose) Polymerases Poly [ADP-Ribose] Polymerase 2 Sequence Alignment DNA Damage |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1999, 274 (25), pp.17860-17868. ⟨10.1074/jbc.274.25.17860⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.274.25.17860 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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