Advertisement

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

  • Hanspeter Naegeli
  • Felix R. Althaus
Conference paper

Abstract

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).

Keywords

Proteolytic Fragment Nucleosomal Core Particle Polymer Size Bovine Carbonic Anhydrase Polymer Pattern 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  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

Personalised recommendations