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DNA-Poly(ADP-Ribose) Polymerase Complex: Isolation of the DNA Wrapping the Enzyme Molecule

  • Marie E. Ittel
  • Jenny Jongstra-Bilen
  • Claude Niedergang
  • Paul Mandel
  • Etienne Delain
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Since the discovery of poly(ADP-ribose) it has been known that DNA is required for the synthesis of the polymer from NAD+ [1, 2]. It was confirmed later with purified poly(ADP-ribose) polymerase that double-stranded DNA is necessary to express its activity in vitro [3–7], Covalently-closed circular double-stranded DNA does not have any effect on the enzyme activity [7, 8]. It has been found by Ohgushi et al. [8] that the relative efficiency of enzyme activation by various DNA samples is closely related to their capacity to bind to the enzyme. These authors have suggested that poly(ADP-ribose) polymerase is activated by, and binds to, nicks or ends on the DNA. The highly purified calf thymus poly(ADP-ribose) polymerase preparation obtained in our laboratory [9, 10] contains a fraction of DNA, called sDNA, which has been shown to activate the enzyme more efficiently than total calf thymus DNA [6]. A DNA fraction called “active DNA” with high enzyme binding and activating capacity has also been isolated during the purification of bovine thymus poly(ADP-ribose) polymerase by Yoshihara and co-workers [5, 11]. The high affinity of this enzyme for the “active DNA” has been attributed to its small size and its high content of nicks [8].

Keywords

Electron Microscopic Observation Enzyme Molecule Micrococcal Nuclease Polymerase Complex Nucleosome Core Particle 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1985

Authors and Affiliations

  • Marie E. Ittel
    • 1
  • Jenny Jongstra-Bilen
    • 2
  • Claude Niedergang
    • 1
  • Paul Mandel
    • 1
  • Etienne Delain
    • 3
  1. 1.Centre de Neurochimie du CNRSStrasbourg CedexFrance
  2. 2.Dept. of Neurobiology, School of MedicineStanford UniversityStanfordUSA
  3. 3.Laboratoire de Microscopie Cellulaire et Moléculaire, LA 147 du CNRSInstitut Gustave RoussyVillejuifFrance

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