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Vol. 15, Issue 2, 734-750, February 2004
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* Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224;
Institute of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, N-7005 Trondheim, Norway;
MRC Radiation and Genome Stability Unit, Harwell, Oxfordshire, OX11 ORD, United Kingdom;
¶ Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York, 14642; and
Department of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad 500 046, India
Submitted August 7, 2003;
Accepted October 9, 2003
Monitoring Editor: Marvin P. Wickens
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 HJ 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.
|| Corresponding author. E-mail address: BroshR{at}grc.nia.nih.gov.
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