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Published 24 October 2005. doi:10.1083/jcb.200502077
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 2, 217-227
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Article

 Analysis of the Xenopus Werner syndrome protein in DNA double-strand break repair

Hong Yan, Jill McCane, Thomas Toczylowski, and Chinyi Chen

Fox Chase Cancer Center, Philadelphia, PA 19111

Correspondence to Hong Yan: Hong_Yan{at}fccc.edu

Werner syndrome is associated with premature aging and increased risk of cancer. Werner syndrome protein (WRN) is a RecQ-type DNA helicase, which seems to participate in DNA replication, double-strand break (DSB) repair, and telomere maintenance; however, its exact function remains elusive. Using Xenopus egg extracts as the model system, we found that Xenopus WRN (xWRN) is recruited to discrete foci upon induction of DSBs. Depletion of xWRN has no significant effect on nonhomologous end-joining of DSB ends, but it causes a significant reduction in the homology-dependent single-strand annealing DSB repair pathway. These results provide the first direct biochemical evidence that links WRN to a specific DSB repair pathway. The assay for single-strand annealing that was developed in this study also provides a powerful biochemical system for mechanistic analysis of homology-dependent DSB repair.

Abbreviations used in this paper: DBS, double-strand break; HR, homologous recombination; NHEJ, nonhomologous end joining; NPE, nucleoplasmic extract; SSA, single-strand annealing; Tet, tetracycline resistance gene; WRN, Werner syndrome protein; WS, Werner syndrome; xWRN, Xenopus WRN.


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