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Poly(ADP-Ribose) Glycohydrolase Activity Causes Recondensation of Relaxed Poly(ADP-Ribosyl)ated Polynucleosomes

  • Gilbert De Murcia
  • Ann Huletsky
  • Daniel Lamarre
  • Alain Gaudreau
  • Jean Pouyet
  • Guy Poirier
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Polyadenosine diphosphate ribose poly(ADP-ribose) polymerase catalyzes the incorporation of the ADP-ribose moiety of NAD into a homopolymer of repeating ADP-ribose units covalently bound to histones and other nuclear protein acceptors [1, 2]. This DNA-dependent enzyme, highly stimulated by nicks and DNA fragmentation [3, 4], is thought to be involved in several basic functions of the chromatin, especially in DNA repair [5–7].

Keywords

Sedimentation Coefficient Diphosphate Ribose Polymerase Molecule Chromatin Sample Adenosine Diphosphate Ribose 
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

  • Gilbert De Murcia
    • 1
  • Ann Huletsky
    • 2
  • Daniel Lamarre
    • 2
  • Alain Gaudreau
    • 2
  • Jean Pouyet
    • 1
  • Guy Poirier
    • 2
  1. 1.Laboratoire de BiophysiqueIBMC du CNRSStrasbourg CédexFrance
  2. 2.Faculté des SciencesUniversité de SherbrookeSherbrookeCanada

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