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Papers In Press, published online ahead of print March 27, 2003
J. Biol. Chem, 10.1074/jbc.M213103200
Submitted on December 23, 2002
Revised on March 13, 2003
Accepted on March 27, 2003

The Werner syndrome protein stimulates DNA polymerase beta strand displacement synthesis via its helicase activity

Jeanine A. Harrigan, Patricia L. Opresko, Cayetano von Kobbe, Padmini S. Kedar, Rajendra Prasad, Samuel H. Wilson, and Vilhelm A. Bohr

Laboratory of Molecular Gerontology, National Institute on Aging, NIH, Baltimore, MD 21224

Corresponding Author: vbohr{at}nih.gov

Werner syndrome is a hereditary premature aging disorder characterized by genomic instability. Genetic analysis and protein interaction studies indicate that the defective gene product (WRN) may play an important role in DNA replication, recombination, and repair. DNA polymerase Beta (Pol beta) is a central participant in both short and long-patch base excision repair (BER) pathways which function to process most spontaneous, alkylated, and oxidative DNA damage. We report here a physical interaction between WRN and Pol Beta, and using purified proteins, reconstitute a portion of the long-patch BER pathway to examine a potential role for WRN in this repair re-sponse. We demonstrate that WRN stimulates Pol beta strand displacement DNA synthesis and that this stimulation is dependent on the helicase activity of WRN. In addition, a truncated WRN protein, containing primarily the helicase domain, retains helicase activity and is sufficient to mediate the stimulation of Pol beta. The WRN helicase also unwinds a BER substrate, providing evidence that WRN plays a role in unwinding DNA repair intermediates. Based on these find-ings, we propose a novel mechanism by which WRN may mediate Pol beta-directed long patch BER.


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