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)


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].


Sedimentation Coefficient Diphosphate Ribose Polymerase Molecule Chromatin Sample Adenosine Diphosphate Ribose 
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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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