HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 283, Issue 36, 24837-24847, September 5, 2008

This Article Full Text Full Text (PDF) All Versions of this Article: 283/36/24837    most recent M802002200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Manfredi, C. Articles by Alonso, J. C. Search for Related Content PubMed PubMed Citation Articles by Manfredi, C. Articles by Alonso, J. C. Social Bookmarking                      What's this?

Bacillus subtilis RecO Nucleates RecA onto SsbA-coated Single-stranded DNA^*

From the Department of Microbial Biotechnology, Centro Nacional de Biotecnología, CSIC, C/Darwin 3, Campus Universidad Autónoma de Madrid, 28049 Madrid, Spain

Subsaturating amounts of Bacillus subtilis SsbA, independently of the order of addition, partially inhibit the single-stranded DNA-dependent dATPase activity of RecA. This negative effect is fully overcome when a substoichiometric amount of RecO is added. SsbA added prior to RecA does not stimulate the dATP-dependent DNA strand exchange activity; however, added after RecA it enhances the extent of strand exchange. The addition of RecO stimulates RecA-mediated joint molecule formation, although it limits the accumulation of final recombination products. Thus we suggest that RecO has a dual activity: RecO acts as a RecA mediator enabling RecA to utilize SsbA-coated single-stranded DNA as a polymerization substrate and controls RecA-mediated DNA strand exchange by limiting its extent. We herein discuss the possible mechanisms of RecO involvement in the regulation of double strand break repair and genetic transformation.

Received for publication, March 12, 2008 , and in revised form, May 28, 2008.

^* This work was supported by Ministerio de Ciencia e Innovación (MCI), Dirección General de Investigación (DGI) Grant BFU2006-01062 (to J. C. A.) and BFU2006-02907 from MCI-DGI (to S. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipient of Ministerio de Educación y Ciencia-DGI Fellowship BMC2003-00150.

² To whom correspondence should be addressed. Fax: 34-91585-4506; E-mail: jcalonso{at}cnb.csic.es.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				P. P. Cardenas, B. Carrasco, H. Sanchez, G. Deikus, D. H Bechhofer, and J. C Alonso Bacillus subtilis polynucleotide phosphorylase 3'-to-5' DNase activity is involved in DNA repair Nucleic Acids Res., July 1, 2009; 37(12): 4157 - 4169. [Abstract] [Full Text] [PDF]