A bacterial arginine-agmatine exchange transporter involved in extreme Acid resistance.
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 approximately 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) approximately 80 mum for Arg, in the same range as its dissociation constant determined by isothermal titration calorimetry.[1]References
- A bacterial arginine-agmatine exchange transporter involved in extreme Acid resistance. Fang, Y., Kolmakova-Partensky, L., Miller, C. J. Biol. Chem. (2007) [Pubmed]
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