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Originally published In Press as doi:10.1074/jbc.M006508200 on July 27, 2000

J. Biol. Chem., Vol. 275, Issue 40, 31024-31029, October 6, 2000
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Transcriptional Activation of an Escherichia coli Copper Efflux Regulon by the Chromosomal MerR Homologue, CueR*

F. Wayne OuttenDagger , Caryn E. Outten§, Jeremy HaleDagger , and Thomas V. O'HalloranDagger §

From the Dagger  Department of Biochemistry, Molecular Biology, and Cell Biology and the § Department of Chemistry, Northwestern University, Evanston, Illinois 60208

Because copper ions are both essential cofactors and cytotoxic agents, the net accumulation of this element in a cell must be carefully balanced. Depending upon the cellular copper status, copper ions must either be imported or ejected. CopA, the principal copper efflux ATPase in Escherichia coli, is induced by elevated copper in the medium, but the copper-sensing regulatory factor is unknown. Inspection of the copA promoter reveals signature elements of promoters controlled by metalloregulatory proteins in the MerR family. These same elements are also present upstream of yacK, which encodes a putative multi-copper oxidase. Homologues of YacK are found in copper resistance determinants that facilitate copper efflux. Here we show by targeted gene deletion and promoter fusion assays that both copA and yacK are regulated in a copper-responsive manner by the MerR homologue, ybbI. We have designated ybbI as cueR for the Cu efflux regulator. This represents the first example of a copper-responsive regulon on the E. coli chromosome and further extends the roles of MerR family members in prokaryotic stress response.

* This work was supported in part by National Institutes of Health Grants R01 GM38784 (to T. V. O.), T32 GM08382 (to C. E. O.), and T32 GM08061 (to F. W. O.).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.

To whom correspondence should be addressed: Dept. of Chemistry, Northwestern University, 2145 Sheridan Rd., Evanston, IL 60208-3113. Tel.: 847-491-5060; Fax: 847-491-7713; E-mail: t-ohalloran@northwestern.edu.

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