Nucleic Acids Research Advance Access originally published online on September 26, 2006
Nucleic Acids Research 2006 34(18):5217-5231; doi:10.1093/nar/gkl677
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Nucleic Acids Research, 2006, Vol. 34, No. 18 5217-5231
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Nucleic Acid Enzymes |
Human RECQ5ß helicase promotes strand exchange on synthetic DNA structures resembling a stalled replication fork
Institute of Molecular Cancer Research, University of Zurich Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
*To whom correspondence should be addressed. Tel: +41 44 635 3470; Fax: +41 44 635 3484; Email: pjanscak{at}imcr.unizh.ch
Received July 25, 2006. Revised August 30, 2006. Accepted September 4, 2006.
The role of the human RECQ5ß helicase in the maintenance of genomic stability remains elusive. Here we show that RECQ5ß promotes strand exchange between arms of synthetic forked DNA structures resembling a stalled replication fork in a reaction dependent on ATP hydrolysis. BLM and WRN can also promote strand exchange on these structures. However, in the presence of human replication protein A (hRPA), the action of these RecQ-type helicases is strongly biased towards unwinding of the parental duplex, an effect not seen with RECQ5ß. A domain within the non-conserved portion of RECQ5ß is identified as being important for its ability to unwind the lagging-strand arm and to promote strand exchange on hRPA-coated forked structures. We also show that RECQ5ß associates with DNA replication factories in S phase nuclei and persists at the sites of stalled replication forks after exposure of cells to UV irradiation. Moreover, RECQ5ß is found to physically interact with the polymerase processivity factor proliferating cell nuclear antigen in vitro and in vivo. Collectively, these findings suggest that RECQ5ß may promote regression of stalled replication forks to facilitate the bypass of replication-blocking lesions by template-switching. Loss of such activity could explain the elevated level of mitotic crossovers observed in RECQ5ß-deficient cells.
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