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Nucleic Acids Research Advance Access originally published online on August 21, 2009
Nucleic Acids Research 2009 37(19):6491-6502; doi:10.1093/nar/gkp671
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Nucleic Acids Research, 2009, Vol. 37, No. 19 6491-6502
© The Author 2009. Published by Oxford University Press.
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 Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks

Tresa George, Qin Wen, Richard Griffiths, Anil Ganesh, Mark Meuth and Cyril M. Sanders*

Institute for Cancer Studies, University of Sheffield, Beech Hill Road, Sheffield, S10 2RX, UK

*To whom correspondence should be addressed. Tel: +44 114 271 2482/3288; Fax: +44 114 271 3515; Email: c.m.sanders{at}sheffield.ac.uk

Received June 19, 2009. Revised July 28, 2009. Accepted July 29, 2009.

Pif-1 proteins are 5'->3' superfamily 1 (SF1) helicases that in yeast have roles in the maintenance of mitochondrial and nuclear genome stability. The functions and activities of the human enzyme (hPif1) are unclear, but here we describe its DNA binding and DNA remodeling activities. We demonstrate that hPif1 specifically recognizes and unwinds DNA structures resembling putative stalled replication forks. Notably, the enzyme requires both arms of the replication fork-like structure to initiate efficient unwinding of the putative leading replication strand of such substrates. This DNA structure-specific mode of initiation of unwinding is intrinsic to the conserved core helicase domain (hPifHD) that also possesses a strand annealing activity as has been demonstrated for the RecQ family of helicases. The result of hPif1 helicase action at stalled DNA replication forks would generate free 3' ends and ssDNA that could potentially be used to assist replication restart in conjunction with its strand annealing activity.


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