PMID:17099215
| Citation |
Fang, Y, Kolmakova-Partensky, L and Miller, C (2007) A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance. J. Biol. Chem. 282:176-82 |
|---|---|
| Abstract |
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 microm for Arg, in the same range as its dissociation constant determined by isothermal titration calorimetry. |
| Links |
PubMed Online version:10.1074/jbc.M610075200 |
| Keywords |
Agmatine/chemistry; Amino Acid Transport Systems/metabolism; Antiporters/metabolism; Arginine/chemistry; Bacterial Physiological Phenomena; Catalysis; Cross-Linking Reagents/pharmacology; Dimerization; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Glutaral/chemistry; Hydrogen-Ion Concentration; Lipids/chemistry; Liposomes/chemistry; Micelles; Models, Biological; Protein Binding |
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