Interaction of poly(ADP-ribose)polymerase with DNA polymerase α
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 wordsDNA polymerase α poly(ADP-ribose)polymerase immunoprecipitation autopoly(ADP-ribosyl)ation
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- 7.Anachkova B, Russev G, Poirier GG: DNA replication and poly(ADP-ribosyl)ation of chromatin. Cytobios 59: 19–28, 1989Google Scholar
- 10.Tanaka Y, Yoshihara K, Itaya A, Kamiya T, Koide S: Mechanism of inhibition of Ca2+, Mg2+-dependent endonuclease of bull seminal plasma by ADP-ribosylation. J Biol Chem 259: 6579–6585, 1990Google Scholar
- 21.Itoh S, Shizuta Y, Hayishi O: Purification and characterization of poly(ADP-ribose) synthetase from calf thymus. J Biol Chem 254: 3647–3651, 1979Google Scholar
- 28.Yamanaka H, Penning A, Willis H, Wasson B, Carson DA: Characterization of human poly (ADP-ribose) polymerase with autoantibodies. J Biol Chem 263: 3879–3883, 1983Google Scholar