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Originally published In Press as doi:10.1074/jbc.M002232200 on April 27, 2000

J. Biol. Chem., Vol. 275, Issue 26, 19735-19741, June 30, 2000
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Regulation of High Affinity Nickel Uptake in Bacteria
Ni2+-DEPENDENT INTERACTION OF NikR WITH WILD-TYPE AND MUTANT OPERATOR SITES*

Peter T. ChiversDagger and Robert T. Sauer§

From the Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Escherichia coli actively imports nickel via the ATP-dependent NikABCDE permease. NikR, a protein of the ribbon-helix-helix family of transcription factors, represses expression of the nikABCDE operon in the presence of excessive concentrations of intracellular nickel. Here, the NikR operator site is identified within the nikABCDE promoter by footprinting and mutational analyses. The operator consists of two dyad-symmetric 5'-GTATGA-3' recognition sequences separated by 16 base pairs. Mutations in the GTATGA sequences reduce NikR binding affinity in vitro and reduce repression of a Pnik-lacZ fusion in vivo. Moreover, NikR is shown to be a direct sensor of nickel ions. Strong operator binding requires the continual presence of 20-50 µM nickel, indicating the presence of a low affinity nickel-binding site, and NikR dimers also contain two high affinity nickel-binding sites. In addition to both GTATGA sites and nickel, high affinity operator binding also requires the C-terminal domain of NikR.

* This work was supported by National Institutes of Health Grants AI-15706 and AI-16892.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 Supported by Natural Sciences and Engineering Research Council (Canada) postdoctoral fellowship.

§ To whom correspondence should be addressed: 68-571, 77 Massachusetts Ave., Cambridge, MA 02139. E-mail: bobsauer@mit.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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