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Nucleic Acids Research 2006 34(1):295-304; doi:10.1093/nar/gkj410
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Published online 12 January 2006

© The Author 2006. 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}oxfordjournals.org

Article

Cockayne syndrome group B protein has novel strand annealing and exchange activities

Meltem Muftuoglu1, Sudha Sharma1, Tina Thorslund2, Tinna Stevnsner2, Martin M. Soerensen1,2, Robert M. Brosh, Jr1 and Vilhelm A. Bohr1,*

1Laboratory of Molecular Gerontology, National Institute on Aging, NIH Baltimore, MD 21224, USA 2Department of Molecular Biology, Danish Center for Molecular Gerontology, University of Aarhus Denmark

*To whom correspondence should be addressed. Tel: +1 410 558 8162; Fax: +1 410 558 8157; Email: vbohr{at}nih.gov

Received October 20, 2005. Revised November 22, 2005. Accepted December 6, 2005.

Cockayne syndrome (CS) is a rare inherited human genetic disorder characterized by UV sensitivity, severe neurological abnormalities and prageroid symptoms. The CS complementation group B (CSB) protein is involved in UV-induced transcription coupled repair (TCR), base excision repair and general transcription. CSB also has a DNA-dependent ATPase activity that may play a role in remodeling chromatin in vivo. This study reports the novel finding that CSB catalyzes the annealing of complementary single-stranded DNA (ssDNA) molecules with high efficiency, and has strand exchange activity. The rate of CSB-catalyzed annealing of complementary ssDNA is 25-fold faster than the rate of spontaneous ssDNA annealing under identical in vitro conditions and the reaction occurs with a high specificity in the presence of excess non-homologous ssDNA. The specificity and intrinsic nature of the reaction is also confirmed by the observation that it is stimulated by dephosphorylation of CSB, which occurs after UV-induced DNA damage, and is inhibited in the presence of ATP{gamma}S. Potential roles of CSB in cooperation with strand annealing and exchange activities for TCR and homologous recombination are discussed.


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