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The nitrite transport protein NirC from Salmonella typhimurium is a nitrite/proton antiporter

MPG-Autoren
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Rycovska,  Adriana
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hatahet,  Lina
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Fendler,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Rycovska, A., Hatahet, L., Fendler, K., & Michel, H. (2012). The nitrite transport protein NirC from Salmonella typhimurium is a nitrite/proton antiporter. Biochimica et Biophysica Acta - Biomembranes, 1818(5), 1342-1350.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-D56B-9
Zusammenfassung
In anaerobically grown bacteria, transport of nitrite is catalyzed by an integral membrane protein of the form ate-nitrite transporter family, NirC, which in Salmonella typhimurium plays a critical role in intracellular virulence. We present a functional characterization of the S. typhimurium nitrite transporter StmNirC in native membrane vesicles as well as purified and reconstituted into proteoliposomes. Using an electrophysiological technique based on solid supported membranes, we show nitrite induced translocation of negative charges into proteoliposomes reconstituted with purified StmNirC. These data demonstrate the electrogenicity of StmNirC and its substrate specificity for nitrite. Monitoring changes in ΔpH on everted membrane vesicles containing overexpressed StmNirC using acridine orange as a pH indicator we demonstrate that StmNirC acts as a secondary active transporter. It promotes low affinity transport of nitrite coupled to H+ antiport with a pH independent profile in the pH range from 6 to 8. In addition to nitrite also nitrate is transported by StmNirC, but with reduced flux and complete absence of proton antiport activity. Taken together, these data suggest a bispecific anion selectivity of StmNirC with an ion specific transport mode. This may play a role in regulating nitrite transport under physiological conditions.