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ADP-Ribosylation of Topoisomerase II in Physiological Conditions

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ADP-Ribosylation Reactions

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Abstract

ADP-ribosylation is known to play an important role in the modulation of chromatin structure, possibly by changing the affinity of histones to DNA and by interfering with the activity of enzymes which are responsible for condensation and decondensation processes (1, 2). Several nuclear proteins have been found to be ADP-ribosylated in reconstituted systems (for a review, see 1). However, it is not yet clear which are the real acceptors in physiological conditions. In fact, beside poly(ADP-ribose)polymerase itself (3, 4), only histones (5), topoisomerase I (6, 7) and high and low mobility group proteins (8) have been recognized to be modified by poly(ADP-ribose) in intact eukaryotic systems.

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Author information

Authors and Affiliations

  1. Istituto Genetica Biochimica Evoluzionistica CNR, Pavia, 27100, Italy

    A. I. Scovassi, M. Negroni, C. Mariani, C. Negri & U. Bertazzoni

  2. Joint Research Center CEC, Ispra, 21027, Italy

    L. Clerici

Authors
  1. A. I. Scovassi
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  2. M. Negroni
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  3. C. Mariani
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  4. L. Clerici
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  5. C. Negri
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  6. U. Bertazzoni
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Editor information

Editors and Affiliations

  1. Centre de Recherches en Endocrinologie Moleculaire, Le Centre Hospitalier de l’Universite Laval, Quebec, G1V 4G2, Canada

    Guy G. Poirier

  2. Biochemistry Department Pavillon Vachon, Universite Laval, Quebec, G1K 7P4, Canada

    Pierre Moreau

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© 1992 Springer Science+Business Media New York

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Scovassi, A.I., Negroni, M., Mariani, C., Clerici, L., Negri, C., Bertazzoni, U. (1992). ADP-Ribosylation of Topoisomerase II in Physiological Conditions. In: Poirier, G.G., Moreau, P. (eds) ADP-Ribosylation Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-8718-1_47

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  • DOI: https://doi.org/10.1007/978-1-4419-8718-1_47

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-6456-9

  • Online ISBN: 978-1-4419-8718-1

  • eBook Packages: Springer Book Archive

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