Histones Affect Polymer Patterns Produced by Poly(ADP-ribose)polymerase

  • Hanspeter Naegeli
  • Felix R. Althaus
Conference paper


The post-translational poly ADP-ribosylation of proteins involves a complex pattern of ADP-ribose polymers. Several variables in these polymers, such as polymer numbers, polymer sizes, and branching frequencies may be important for differentially regulating the function of a given protein. Little is known about the molecular factors regulating these parameters (for review see 1,2,3).


Proteolytic Fragment Nucleosomal Core Particle Polymer Size Bovine Carbonic Anhydrase Polymer Pattern 
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  1. 1.
    Ueda, K. (1986) In Pyridine Nucleotide Coenzymes (Dolphin, D., Poulson, R. & Avramovic, O., eds.) Part B pp. 549–597, John Wiley & Sons, New YorkGoogle Scholar
  2. 2.
    Althaus, F.R. & Richter, C. (1987) ADP-ribo.syiation of Proteins: Enzymology and Biological Significance, Springer-Verlag, BerlinCrossRefGoogle Scholar
  3. 3.
    Jacobson, M.K. & Jacobson, E.L. (1989) ADP-ribose Transfer Reactions: Mechanisms and Biological Significance, Springer-Verlag, BerlinCrossRefGoogle Scholar
  4. 4.
    Naegeli, H., Loetscher, P. & Althaus, FR. (1989) J. Biol. Chem. 264, 14382–14385PubMedGoogle Scholar
  5. 5.
    . Naegeli, H. & Althaus, F.R. (1991) J. Biol. Chem. 266, in press Google Scholar
  6. 6.
    Kawamura, M., Tanigawa, Y., Kitamura, A., Miyake, Y. & Shimoyama, M. (1981) Biochim. Biophys. Acta 652, 121–128PubMedCrossRefGoogle Scholar
  7. 7.
    Tanaka, Y., Hashida, T., Yoshihara, H. & Yoshihara, K. (1979) J. Biol. Chem. 254, 12433–12438PubMedGoogle Scholar
  8. 8.
    Ferro, A.M. & Olivera, M.O. (1982) J. Biol. Chem. 257, 7808–7813PubMedGoogle Scholar
  9. 9.
    . Hartman, P.G., Chapman, G.E., Moss, T. & Bradbury, E.M. (1977) Ear. J. Biochim. 77, 45–51 CrossRefGoogle Scholar
  10. l0.
    Bradbury, E.M., Chapman, G.E., Danby, S.E., Hartman, P.G. & Riches, P.L. (1975) Eur. J. Biochim. 57, 521–528Google Scholar
  11. 11.
    Thoma, F., Lose, R. & Koller, T. (1983) J. Mol. Biol. 167, 619–640CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Hanspeter Naegeli
    • 1
  • Felix R. Althaus
    • 1
  1. 1.University of Zürich-Tierspital, Institute of Pharmacology & BiochemistryZürichSwitzerland

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