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Nucleic Acids Research 2005 33(12):3932-3941; doi:10.1093/nar/gki712
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Published online 15 July 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

The Bloom's syndrome helicase promotes the annealing of complementary single-stranded DNA

Chit Fang Cheok, Leonard Wu, Patrick L. Garcia1, Pavel Janscak1 and Ian D. Hickson*

Cancer Research UK Laboratories, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital Oxford OX3 9DS, UK 1Institute of Molecular Cancer Research, University of Zürich August Forel-Strasse 7, CH-8008, Zürich, Switzerland

*To whom correspondence should be addressed. Tel: +44 0 1865 222 417; Fax: +44 0 1865 222 431; Email: ian.hickson{at}cancer.org.uk

Received May 31, 2005. Revised June 30, 2005. Accepted June 30, 2005.

The product of the gene mutated in Bloom's syndrome, BLM, is a 3'–5' DNA helicase belonging to the highly conserved RecQ family. In addition to a conventional DNA strand separation activity, BLM catalyzes both the disruption of non-B-form DNA, such as G-quadruplexes, and the branch migration of Holliday junctions. Here, we have characterized a new activity for BLM: the promotion of single-stranded DNA (ssDNA) annealing. This activity does not require Mg2+, is inhibited by ssDNA binding proteins and ATP, and is dependent on DNA length. Through analysis of various truncation mutants of BLM, we show that the C-terminal domain is essential for strand annealing and identify a 60 amino acid stretch of this domain as being important for both ssDNA binding and strand annealing. We present a model in which the ssDNA annealing activity of BLM facilitates its role in the processing of DNA intermediates that arise during repair of damaged replication forks.


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