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Sagot :
By decarboxylating arginine, Escherichia coli's severe acid resistance response is arginine-dependent.
A proton is actually exported with each turnover of the membrane antiporter AdiC, which catalyzes the decarboxylation product agmatine's efflux together with arginine influx.
Extreme acid resistance is facilitated by a bacterial arginine-agmatine exchange transporter.
- We produced and purified the transport protein using the adiC coding sequence under the control of a tetracycline promoter in an E. coli vector, with a yield of roughly 10 mg/liter bacterial culture.
- In detergent micelles and lipid membranes, the protein is a homodimer, according to tests using the cross-linking of glutaraldehyde.
- In liposome form, purified AdiC exchanges arginine and agmatine in a closely linked, electrogenic manner.
- The dissociation constant for Arg, as calculated by isothermal titration calorimetry, is in the same range as the K(m) value obtained through kinetic analysis, which is around 80 microm.
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