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Originally published In Press as doi:10.1074/jbc.M204122200 on June 20, 2002

J. Biol. Chem., Vol. 277, Issue 36, 32714-32721, September 6, 2002
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The Linker Region Plays an Important Role in the Interdomain Communication of the Response Regulator OmpR*

Kirsten MattisonDagger , Ricardo Oropeza§, and Linda J. Kenney

From the Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, Oregon 97239

OmpR is the response regulator of a two-component regulatory system that controls the expression of the porin genes ompF and ompC in Escherichia coli. This regulator consists of two domains joined by a flexible linker region. The amino-terminal domain is phosphorylated by the sensor kinase EnvZ, and the carboxyl-terminal domain binds DNA via a winged helix-turn-helix motif. In vitro studies have shown that amino-terminal phosphorylation enhances the DNA binding affinity of OmpR and, conversely, that DNA binding by the carboxyl terminus increases OmpR phosphorylation. In the present work, we demonstrate that the linker region contributes to this communication between the two domains of OmpR. Changing the specific amino acid composition of the linker alters OmpR function, as does increasing or decreasing its length. Three linker mutants give rise to an OmpF+ OmpC- phenotype, but the defects are not due to a shared molecular mechanism. Currently, functional homology between response regulators is predicted based on similarities in the amino and carboxyl-terminal domains. The results presented here indicate that linker length and composition should also be considered. Furthermore, classification of response regulators in the same subfamily does not necessarily imply that they share a common response mechanism.

* This work was supported by National Science Foundation Grant MCB-9904658 and National Institutes of Health Grant GM-58746 (to L. J. 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.

Dagger Predoctoral fellow of the American Heart Association-Northwest Affiliate.

§ Recipient of a Consejo Nacional de Cientificas y Tecnicas (CONACyT) fellowship from the Mexican government. Current address: Instituto de Biotecnologia, Universidad Nacional Autonoma de Mexico, Ave. Universidad 2001, Cuernavaca, Morelos, 62210 Mexico.

To whom correspondence should be addressed: Dept. of Molecular Microbiology and Immunology, L-220, Oregon Health and Science University, 3181 S. W. Sam Jackson Park Rd., Portland, OR 97239. Tel.: 503-494-1363; Fax: 503-494-6862; E-mail: KenneyL@ohsu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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