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J. Biol. Chem., Vol. 279, Issue 51, 52991-52997, December 17, 2004

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Inhibition of RecA Protein by the Escherichia coli RecX Protein

MODULATION BY THE RecA C TERMINUS AND FILAMENT FUNCTIONAL STATE^*

Julia C. Drees, Shelley L. Lusetti, and Michael M. Cox

From the Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544

The RecX protein is a potent inhibitor of RecA activities. We identified several factors that affect RecX-RecA interaction. The interaction is enhanced by the RecA C terminus and by significant concentrations of free Mg²⁺ ion. The interaction is also enhanced by an N-terminal His₆ tag on the RecX protein. We conclude that RecX protein interacts most effectively with a RecA functional state designated A_o and that the RecA C terminus has a role in modulating the interaction. We further identified a C-terminal point mutation in RecA protein (E343K) that significantly alters the interaction between RecA and RecX proteins.

Received for publication, August 6, 2004 , and in revised form, October 4, 2004.

^* This work was supported by Grant GM 52725 from the National Institutes of Health (to M. M. C.). 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.

To whom correspondence should be addressed: Dept. of Biochemistry, University of Wisconsin-Madison, 433 Babcock Dr., Madison, WI 53706-1544. Tel.: 608-262-1181; Fax: 608-265-2603; E-mail: cox{at}biochem.wisc.edu.

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