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Nucleic Acids Research 2005 33(5):1662-1670; doi:10.1093/nar/gki310
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Published online 21 March 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

Single-stranded DNA-binding protein of Deinococcus radiodurans: a biophysical characterization

Gregor Witte, Claus Urbanke and Ute Curth*

Department of Biophysical Chemistry, Medical School Hannover Hannover, Germany

*To whom correspondence should be addressed at Medizinische Hochschule Hannover, Zentrale Einrichtung für biophysikalisch-biochemische Verfahren, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany. Tel: +49 511 532 3707; Fax: +49 511 532 5966; Email: curth.ute{at}mh-hannover.de

Received January 28, 2005. Revised February 28, 2005. Accepted February 28, 2005.

The highly conserved bacterial single-stranded DNA-binding (SSB) proteins play an important role in DNA replication, repair and recombination and are essential for the survival of the cell. They are functional as tetramers, in which four OB(oligonucleotide/oligosaccharide binding)-folds act as DNA-binding domains. The protomer of the SSB protein from the extremely radiation-resistant organism Deinococcus radiodurans (DraSSB) has twice the size of the other bacterial SSB proteins and contains two OB-folds. Using analytical ultracentrifugation, we could show that DraSSB forms globular dimers with some protrusions. These DraSSB dimers can interact with two molecules of E.coli DNA polymerase III {chi} subunit. In fluorescence titrations with poly(dT) DraSSB bound 47–54 nt depending on the salt concentration, and fluorescence was quenched by more than 75%. A distinct low salt binding mode as for EcoSSB was not observed for DraSSB. Nucleic acid binding affinity, rate constant and association mechanism are quite similar for EcoSSB and DraSSB. In a complementation assay in E.coli, DraSSB took over the in vivo function of EcoSSB. With DraSSB behaving almost identical to EcoSSB the question remains open as to why dimeric SSB proteins have evolved in the Thermus group of bacteria.

DDBJ/EMBL/GenBank accession no. AJ564860


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