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J. Biol. Chem., Vol. 282, Issue 1, 176-182, January 5, 2007

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A Bacterial Arginine-Agmatine Exchange Transporter Involved in Extreme Acid Resistance^*

From the Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454

The arginine-dependent extreme acid resistance response of Escherichia coli operates by decarboxylating arginine. AdiC, a membrane antiporter, catalyzes arginine influx coupled to efflux of the decarboxylation product agmatine, effectively exporting a proton in each turnover. Using the adiC coding sequence under control of a tetracycline promoter in an E. coli vector, we expressed and purified the transport-protein with a yield of 10 mg/liter bacterial culture. Glutaraldehyde cross-linking experiments indicate that the protein is a homodimer in detergent micelles and lipid membranes. Purified AdiC reconstituted into liposomes exchanges arginine and agmatine in a strictly coupled, electrogenic fashion. Kinetic analysis yields K_m 80 µM for Arg, in the same range as its dissociation constant determined by isothermal titration calorimetry.

Received for publication, October 27, 2006 , and in revised form, November 7, 2006.

^* 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.

¹ To whom correspondence should be addressed: Brandeis University, Biochemistry Dept., 415 South St., Waltham, MA 02468. Tel.: 781-736-2340; Fax: 781-736-2365; E-mail: cmiller{at}brandeis.edu.

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