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Nucleic Acids Research 2006 34(4):1084-1091; doi:10.1093/nar/gkj503
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Published online 18 February 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

RecJ exonuclease: substrates, products and interaction with SSB

Eugene S. Han, Deani L. Cooper, Nicole S. Persky1, Vincent A. Sutera, Jr, Richard D. Whitaker2, Melissa L. Montello2 and Susan T. Lovett*

Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University Waltham, MA 02454-9110, USA 1Graduate Program in Biophysics and Structural Biology, Brandeis University Waltham, MA 02454-9110, USA 2New England Biolabs, Inc. 240 Country Road Ipswich, MA 01938-2723, USA

*To whom correspondence should be addressed. Tel: +1 781 736 2497; Fax: +1 781 736 2405; Email: lovett{at}brandeis.edu

Received December 23, 2005. Revised January 25, 2006. Accepted January 25, 2006.

The RecJ exonuclease from Escherichia coli degrades single-stranded DNA (ssDNA) in the 5'–3' direction and participates in homologous recombination and mismatch repair. The experiments described here address RecJ's substrate requirements and reaction products. RecJ complexes on a variety of 5' single-strand tailed substrates were analyzed by electrophoretic mobility shift in the absence of Mg2+ ion required for substrate degradation. RecJ required single-stranded tails of 7 nt or greater for robust binding; addition of Mg2+ confirmed that substrates with 5' tails of 6 nt or less were poor substrates for RecJ exonuclease. RecJ is a processive exonuclease, degrading ~1000 nt after a single binding event to single-strand DNA, and releases mononucleotide products. RecJ is capable of degrading a single-stranded tail up to a double-stranded junction, although products in such reactions were heterogeneous and RecJ showed a limited ability to penetrate the duplex region. RecJ exonuclease was equally potent on 5' phosphorylated and unphosphorylated ends. Finally, DNA binding and nuclease activity of RecJ was specifically enhanced by the pre-addition of ssDNA-binding protein and we propose that this specific interaction may aid recruitment of RecJ.


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