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A more recent version of this article appeared on February 1, 2004
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Submitted on August 7, 2003
Accepted on October 9, 2003
1 Laboratory of Molecular Gerontology, National Institute on Aging, NIH, 5600 Nathan Shock Drive, Baltimore, Maryland 21224 USA, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad 500 046 India
2 Institute of Cancer Research and Molecular Medicine, Norweigian University of Science and Technology, Olav Kyrresgate 3, N-7005 Trondheim, Norway
3 Laboratory of Molecular Gerontology, National Institute on Aging, NIH, 5600 Nathan Shock Drive, Baltimore, Maryland 21224 USA
4 MRC Radiation & Genome Stability Unit, Harwell, Oxfordshire, OX11 ORD, UK
5 Department of Biochemistry & Biophysics, Box 712, University of Rochester Medical Center, 601 Elmwood Ave., Rochester, New York, 14642 USA
* Corresponding author. E-mail address: BroshR{at}grc.nia.nih.gov.
Werner Syndrome is a premature aging disorder characterized by genomic instability, elevated recombination, and replication defects. It has been hypothesized that defective processing of certain replication fork structures by WRN may contribute to genomic instability. Fluorescence resonance energy transfer (FRET) analyses show that WRN and Flap Endonuclease-1 (FEN-1) form a complex in vivo that colocalizes in foci associated with arrested replication forks. WRN effectively stimulates FEN-1 cleavage of branch-migrating double flap structures that are the physiological substrates of FEN-1 during replication. Biochemical analyses demonstrate that WRN helicase unwinds the chicken-foot Holliday Junction intermediate associated with a regressed replication fork and stimulates FEN-1 to cleave the unwound product in a structure-dependent manner. These results provide evidence for an interaction between WRN and FEN-1 in vivo and suggest that these proteins function together to process DNA structures associated with the replication fork.
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