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Nucleic Acids Research Advance Access originally published online on February 1, 2007
Nucleic Acids Research 2007 35(4):1367-1376; doi:10.1093/nar/gkl831
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Nucleic Acids Research, 2007, Vol. 35, No. 4 1367-1376
© 2007 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.

Nucleic Acid Enzymes

DNA strand displacement, strand annealing and strand swapping by the Drosophila Bloom's syndrome helicase

Brian T. Weinert and Donald C. Rio*

Department of Molecular and Cell Biology, 16 Barker Hall #3204, University of California Berkeley, CA 94720-3204, USA

*To whom correspondence should be addressed. Tel: +1 510 642 1071; Fax: +1 510 642 6062; Email: don_rio{at}berkeley.edu

Received July 19, 2006. Revised October 3, 2006. Accepted October 8, 2006.

Genetic analysis of the Drosophila Bloom's syndrome helicase homolog (mus309/DmBLM) indicates that DmBLM is required for the synthesis-dependent strand annealing (SDSA) pathway of homologous recombination. Here we report the first biochemical study of DmBLM. Recombinant, epitope-tagged DmBLM was expressed in Drosophila cell culture and highly purified protein was prepared from nuclear extracts. Purified DmBLM exists exclusively as a high molecular weight (~1.17 MDa) species, is a DNA-dependent ATPase, has 3'->5' DNA helicase activity, prefers forked substrate DNAs and anneals complementary DNAs. High-affinity DNA binding is ATP-dependent and low-affinity ATP-independent interactions contribute to forked substrate DNA binding and drive strand annealing. DmBLM combines DNA strand displacement with DNA strand annealing to catalyze the displacement of one DNA strand while annealing a second complementary DNA strand.


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