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Nucleic Acids Research Advance Access originally published online on August 25, 2006
Nucleic Acids Research 2006 34(15):4098-4105; doi:10.1093/nar/gkl538
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Nucleic Acids Research, 2006, Vol. 34, No. 15 4098-4105
© 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.

Survey and Summary

Sit down, relax and unwind: structural insights into RecQ helicase mechanisms

Michael P. Killoran and James L. Keck*

Department of Biomolecular Chemistry, 550 Medical Science Center, 1300 University Avenue, University of Wisconsin School of Medicine and Public Health Madison, WI 53706-1532, USA

*To whom correspondence should be addressed. Tel: +1 608 263 1815; Fax: +1 608 262 5253; Email: jlkeck{at}wisc.edu

Received March 28, 2006. Revised June 29, 2006. Accepted July 13, 2006.

Helicases are specialized molecular motors that separate duplex nucleic acids into single strands. The RecQ family of helicases functions at the interface of DNA replication, recombination and repair in bacterial and eukaryotic cells. They are key, multifunctional enzymes that have been linked to three human diseases: Bloom's, Werner's and Rothmund–Thomson's syndromes. This review summarizes recent studies that relate the structures of RecQ proteins to their biochemical activities.


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