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

  • Part II: Poly(ADP-ribosyl)ation
  • A. Structure and Enzymology of Poly(ADP-ribose) Polymerase
  • Published:
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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.

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  1. Laboratory of Cancer Cell Biology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Showa-ku, Nagoya 466, Japan

    Shonen Yoshida & Cynthia Marie G. Simbulan

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  1. Shonen Yoshida
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  2. Cynthia Marie G. Simbulan
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Yoshida, S., Simbulan, C.M.G. Interaction of poly(ADP-ribose)polymerase with DNA polymerase α. Mol Cell Biochem 138, 39–44 (1994). https://doi.org/10.1007/BF00928441

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