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

  • Shonen Yoshida
  • Cynthia Marie G. Simbulan
Part of the Developments in Molecular and Cellular Biochemistry book series (DMCB, volume 12)

Abstract

Homogeneously purified poly(ADP-ribose) polymerase (PARP) specifically stimulated the activity of immunoaffinity-puri-fied calf or human DNA polymerase a by about 6 to 60-fold. Apparently, poly(ADP-ribosyl)ation of DNA polymerase a was not necessary for the stimulation. The effects of PARP on DNA polymerase a 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 a. 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. (Mol Cell Biochem 138: 39–44, 1994)

Key words

DNA polymerase α poly(ADP-ribose)polymerase immunoprecipitation autopoly(ADP-ribosyl)ation 

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Copyright information

© Springer Science+Business Media Dordrecht 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 MedicineShowa-ku, NagoyaJapan

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