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Nucleic Acids Research 2005 33(7):2343-2350; doi:10.1093/nar/gki533
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Published online 22 April 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

Bacillus subtilis RecN binds and protects 3'-single-stranded DNA extensions in the presence of ATP

Humberto Sanchez and Juan C. Alonso*

Department of Microbial Biotechnology, Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid Cantoblanco, 28049 Madrid, Spain

*To whom correspondence should be addressed. Tel: +34 585 4546; Fax: +34 585 4506; Email: jcalonso{at}cnb.uam.es

Received January 31, 2005. Revised March 23, 2005. Accepted April 6, 2005.

Bacillus subtilis RecN appears to be an early detector of breaks in double-stranded DNA. In vivo, RecN forms discrete nucleoid-associated structures and in vitro exhibits Mg2+-dependent single-stranded (ss) DNA binding and ssDNA-dependent ATPase activities. In the presence of ATP or ADP, RecN assembles to form large networks with ssDNA molecules (designated complexes CII and CIII) that involve ATP binding and requires a 3'-OH at the end of ssDNA molecule. Addition of dATP–RecA complexes dissociates RecN from these networks, but this is not observed following addition of an ssDNA binding protein. Apparently, ATP modulates the RecN–ssDNA complex for binding to ssDNA extensions and, in vivo, RecN–ATP bound to 3'-ssDNA might sequester ssDNA ends within complexes that protect the ssDNA while the RecA accessory proteins recruit RecA. With the association of RecA to ssDNA, RecN would dissociate from the DNA end facilitating the subsequent steps in DNA repair.


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This article has been cited by other articles:


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H. Sanchez, P. P. Cardenas, S. H. Yoshimura, K. Takeyasu, and J. C. Alonso
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Recruitment of Bacillus subtilis RecN to DNA Double-Strand Breaks in the Absence of DNA End Processing
J. Bacteriol., January 15, 2006; 188(2): 353 - 360.
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