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Nucleic Acids Research 2005 33(11):3678-3690; doi:10.1093/nar/gki685
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Published online 30 June 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

Archaeal Hel308 helicase targets replication forks in vivo and in vitro and unwinds lagging strands

Colin P. Guy and Edward L. Bolt*

Institute of Genetics, School of Biology, University of Nottingham, Queen's Medical Centre Nottingham NG7 2UH, UK

*To whom correspondence should be addressed. Tel: +44 0115 9709404; Fax: +44 0115 9709906; Email: ed.bolt{at}nottingham.ac.uk

Received May 31, 2005. Revised June 14, 2005. Accepted June 14, 2005.

Mutations in mammalian and Drosophila Hel308 and PolQ paralogues cause genome instability but their helicase functions are mysterious. By in vivo and in vitro analysis, we show that Hel308 from archaea (Hel308a) may act at stalled replication forks. Introducing hel308a into Escherichia coli dnaE strains that conditionally accumulate stalled forks caused synthetic lethality, an effect indistinguishable from E.coli RecQ. Further analysis in vivo indicated that the effect of hel308a is exerted independently of homologous recombination. The minimal biochemical properties of Hel308a protein were the same as human Hel308. We describe how helicase actions of Hel308a at fork structures lead specifically to displacement of lagging strands. The invading strand of D-loops is also targeted. Using archaeal Hel308, we propose models of action for the helicase domain of PolQ, promoting loading of the translesion polymerase domain. We speculate that removal of lagging strands at stalled forks by Hel308 promotes the formation of initiation zones, priming restart of lagging strand synthesis.


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