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Nucleic Acids Research 2005 33(12):3942-3952; doi:10.1093/nar/gki713
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Published online 15 July 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 RecU Holliday-junction resolvase modulates RecA activities

Begoña Carrasco1, Silvia Ayora1,2, Rudi Lurz3 and Juan C. Alonso1,*

1Departmento de Biotecnología Microbiana, Centro Nacional de Biotecnología, CSIC C/Darwin 3, Campus Universidad Autónoma de Madrid, 28049 Madrid, Spain 2Departamento de Biología Molecular C/Darwin 2, Universidad Autónoma de Madrid, 28049 Madrid, Spain 3Max-Planck-Institut für molekulare Genetik Ihnestrasse 73, D-14195, Germany

*To whom correspondence should be addressed. Tel: +34 91585 4546; Fax: +34 91585 4506; Email: jcalonso{at}cnb.uam.es

Received May 17, 2005. Revised June 30, 2005. Accepted June 30, 2005.

The Bacillus subtilis RecU protein is able to catalyze in vitro DNA strand annealing and Holliday-junction resolution. The interaction between the RecA and RecU proteins, in the presence or absence of a single-stranded binding (SSB) protein, was studied. Substoichiometric amounts of RecU enhanced RecA loading onto single-stranded DNA (ssDNA) and stimulated RecA-catalyzed D-loop formation. However, RecU inhibited the RecA-mediated three-strand exchange reaction and ssDNA-dependent dATP or rATP hydrolysis. The addition of an SSB protein did not reverse the negative effect exerted by RecU on RecA function. Annealing of circular ssDNA and homologous linear 3'-tailed double-stranded DNA by RecU was not affected by the addition of RecA both in the presence and in the absence of SSB. We propose that RecU modulates RecA activities by promoting RecA-catalyzed strand invasion and inhibiting RecA-mediated branch migration, by preventing RecA filament disassembly, and suggest a potential mechanism for the control of resolvasome assembly.


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