Molecular and Cellular Biochemistry

, Volume 138, Issue 1, pp 39–44

Interaction of poly(ADP-ribose)polymerase with DNA polymerase α

  • Shonen Yoshida
  • Cynthia Marie G. Simbulan
Part II: Poly(ADP-ribosyl)ation A. Structure and Enzymology of Poly(ADP-ribose) Polymerase

DOI: 10.1007/BF00928441

Cite this article as:
Yoshida, S. & Simbulan, C.M.G. Mol Cell Biochem (1994) 138: 39. doi:10.1007/BF00928441

Abstract

Homogeneously purified poly(ADP-ribose) polymerase (PARP) specifically stimulated the activity of immunoaffinity-purified calf or human DNA polymerase α by about 6 to 60-fold. Apparently, poly(ADP-ribosyl)ation of DNA polymerase α was not necessary for the stimulation. The effects of PARP on DNA polymerase α were biphasic: at very low concentrations of DNA, it rather inhibited its activity, whereas, at higher DNA concentrations, PARP greatly stimulated it. The autopoly(ADP-ribosyl)ation of PARP suppressed both its stimulatory and inhibitory effects. By immunoprecipitation with an anti-DNA polymerase α antibody, it was clearly shown that PARP may be physically associated with DNA polymerase α. Stimulation of DNA polymerase α may be attributed to the physical association between the two, rather than to the DNA-binding capacity of PARP, since the PARP fragment containing only the DNA binding domain showed little stimulatory activity. The existence of PARP-DNA polymerase α complexes were also detected in crude extracts of calf thymus.

Key words

DNA polymerase αpoly(ADP-ribose)polymeraseimmunoprecipitationautopoly(ADP-ribosyl)ation

Copyright information

© Kluwer Academic Publishers 1994

Authors and Affiliations

  • Shonen Yoshida
    • 1
  • Cynthia Marie G. Simbulan
    • 1
  1. 1.Laboratory of Cancer Cell Biology, Research Institute for Disease Mechanism and ControlNagoya University School of MedicineNagoya 466Japan