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Originally published In Press as doi:10.1074/jbc.M210496200 on November 9, 2002

J. Biol. Chem., Vol. 278, Issue 4, 2278-2285, January 24, 2003
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Escherichia coli RecX Inhibits RecA Recombinase and Coprotease Activities in Vitro and in Vivo*

Elizabeth A. StohlDagger §, Joel P. Brockman||, Kristin L. BurkleDagger **, Katsumi Morimatsu, Stephen C. Kowalczykowski, and H. Steven SeifertDagger Dagger Dagger

From the Dagger  Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611 and the  Division of Biological Sciences, Section of Microbiology and of Molecular and Cellular Biology, Center for Genetics and Development, University of California, Davis, California 95616

In Escherichia coli the RecA protein plays a pivotal role in homologous recombination, DNA repair, and SOS repair and mutagenesis. A gene designated recX (or oraA) is present directly downstream of recA in E. coli; however, the function of RecX is unknown. In this work we demonstrated interaction of RecX and RecA in a yeast two-hybrid assay. In vitro, substoichiometric amounts of RecX strongly inhibited both RecA-mediated DNA strand exchange and RecA ATPase activity. In vivo, we showed that recX is under control of the LexA repressor and is up-regulated in response to DNA damage. A loss-of-function mutation in recX resulted in decreased resistance to UV irradiation; however, overexpression of RecX in trans resulted in a greater decrease in UV resistance. Overexpression of RecX inhibited induction of two din (damage-inducible) genes and cleavage of the UmuD and LexA repressor proteins; however, recX inactivation had no effect on any of these processes. Cells overexpressing RecX showed decreased levels of P1 transduction, whereas recX mutation had no effect on P1 transduction frequency. Our combined in vitro and in vivo data indicate that RecX can inhibit both RecA recombinase and coprotease activities.

* This work was supported in part by National Institutes of Health Grants RO1-AI44239 (to H. S. S.) and RO1-GM-62653 (to S. C. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by American Cancer Society postdoctoral fellowship PF-00-016-01-GMMC.

|| Present address: Molecular Staging, Inc., 300 George St., Suite 701, New Haven, CT 06511.

** Present address: Dept. of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153.

Dagger Dagger To whom correspondence should be addressed: Dept. of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, 303 E. Chicago Ave., Chicago, IL 60611. Tel.: 312-503-9788; Fax: 312-503-1339; E-mail: h-seifert@northwestern.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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