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A more recent version of this article appeared on June 29, 2001
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M102125200v1
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Papers In Press, published online ahead of print May 4, 2001
J. Biol. Chem, 10.1074/jbc.M102125200
Submitted on March 9, 2001
Revised on May 2, 2001
Accepted on May 3, 2001

Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate: Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair

Olga I. Lavrik, Rajendra Prasad, Robert W. Sobol, Julie K. Horton, Eric J. Ackerman, and Samuel H. Wilson

NIEHS, Research Triangle Park, NC 27709

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

To examine the interaction of mammalian base excision repair (BER) enzymes with DNA intermediates formed during BER, we used a novel photoaffinity labeling probe and mouse embryonic fibroblast cellular extracts. The probe was formed in situ, using an end-labeled oligonucleotide containing a synthetic abasic site; this site was incised by apurinic/apyrimidinic endonuclease creating a nick with 3' hydroxyl and 5' reduced sugar phosphate groups at the margins, and then a dNMP carrying a photoreactive adduct was added to the 3' hydroxyl group. With near UV-light (312 nm) exposure of the extract-probe mixture, six proteins were strongly labeled. Four of these include poly(ADP-ribose) polymerase-1 (PARP-1) and the BER participants flap endonuclease-1, DNA polymerase beta , and apurinic/apyrimidinic endonuclease. The amount of the probe crosslinked to PARP-1 was greater than that crosslinked to the other proteins. The specificity of PARP-1 labeling was examined using various competitor oligonucleotides and DNA probes with alternate structures. PARP-1 labeling was stronger with a DNA representing a BER intermediate than with a nick in double-stranded DNA. These results indicate that proteins interacting preferentially with a photoreactive BER intermediate can be selected from the crude cellular extract.


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