Less Is More: Neisseria gonorrhoeae RecX Protein Stimulates Recombination by Inhibiting RecA*
- Marielle C. Gruenig‡,
- Elizabeth A. Stohl§,
- Sindhu Chitteni-Pattu‡,
- H. Steven Seifert§ and
- Michael M. Cox‡,1
- From the ‡Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706 and
- the §Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611
- 1 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.
Abstract
Escherichia coli RecX (RecXEc) is a negative regulator of RecA activities both in the bacterial cell and in vitro. In contrast, the Neisseria gonorrhoeae RecX protein (RecXNg) enhances all RecA-related processes in N. gonorrhoeae. Surprisingly, the RecXNg protein is not a RecA protein activator in vitro. Instead, RecXNg is a much more potent inhibitor of all RecANg and RecAEc activities than is the E. coli RecX ortholog. A series of RecXNg mutant proteins representing a gradient of functional deficiencies provide a direct correlation between RecANg inhibition in vitro and the enhancement of RecANg function in N. gonorrhoeae. Unlike RecXEc, RecXNg does not simply cap the growing ends of RecA filaments, but it directly facilitates a more rapid RecA filament disassembly. Thus, in N. gonorrhoeae, recombinational processes are facilitated by RecXNg protein-mediated limitations on RecANg filament presence and/or length to achieve maximal function.
- DNA
- DNA Enzymes
- DNA Recombination
- DNA Repair
- Nucleic Acid Enzymology
- Escherichia coli
- Neisseria gonorrhoeae
- RecA
- RecX
Footnotes
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↵* This work was supported, in whole or in part, by National Institutes of Health Grants GM32335 (to M. M. C.) and R37 AI033493 and R01 AI044239 (to H. S. S.). This work was also supported by the Dr. James Chieh-Hsia Mao and the William R. & Dorothy E. Sullivan Wisconsin Distinguished Graduate Fellowships (to M. C. G.) and partially supported by American Cancer Society Postdoctoral Fellowship PF-00-016-01-GMC (to E. A. S.).
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The on-line version of this article (available at http://www.jbc.org) contains supplemental text, Tables S1–S3, and Figs. S1–S4.
- Received August 3, 2010.
- Revision received September 12, 2010.
- © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.











