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