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A more recent version of this article appeared on August 24, 2001
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C100292200v1
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Papers In Press, published online ahead of print July 5, 2001
J. Biol. Chem, 10.1074/jbc.C100292200
Submitted on June 1, 2001
Revised on July 2, 2001
Accepted on July 3, 2001

DNA Polymerase beta -mediated Long Patch Base Excision Repair: Poly(ADP-ribose) Polymerase-1 Stimulates Strand Displacement DNA Synthesis

Rajendra Prasad, Olga I. Lavrik, Soon-Jong Kim, Padmini Kedar, Xiao-Ping Yang, Brian J. Vande Berg, and Samuel H. Wilson

NIEHS, Research Triangle Park, NC 27709

Corresponding Author: wilson5{at}niehs.nih.gov

The involvement of poly(ADP-ribose) polymerase-1 (PARP-1) in base excision repair (BER) is suggested in several reports, however the role of PARP-1 is still unclear. Recently, photoaffinity labeling experiments with mouse cell extracts suggested that PARP-1 functions as a surveillance protein for a stalled BER intermediate (Lavrik, O.I., Prasad, R., Sobol, R.W., Horton, J.K., Ackerman, E.J., and Wilson, S.H. (2001) J. Biol. Chem. In Press.) To further understand the role of PARP-1 in BER, we examined the DNA synthesis and flap excision steps in long patch BER using a reconstituted system containing a 34-bp BER substrate and five purified human enzymes: uracil-DNA glycosylase, apurinic/apyrimidinic endonuclease, DNA polymerase beta , flap endonuclease-1 (FEN-1) and PARP-1. PARP-1 stimulates strand displacement DNA synthesis by DNA polymerase beta in this system; this stimulation is dependent on the presence of FEN-1. PARP-1 and FEN-1, therefore, cooperate to activate long patch BER. The results are discussed in the context of a model for BER sub-pathway choice, illustrating a dual role for PARP-1 as a surveillance protein for a stalled BER intermediate and an activating factor for long patch BER DNA synthesis.


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