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

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. doi:10.1016/j.bbamem.2012.02.004.

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 Creators:
Rycovska, Adriana1, Author              
Hatahet, Lina2, Author              
Fendler, Klaus2, Author              
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Free keywords: Nitrite transport; Dequenching assay; Acridine orange; Solid supported membrane; Transport mechanism
 Abstract: 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.

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Language(s): eng - English
 Dates: 2012-02-012011-08-122012-02-062012-02-132012-05
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbamem.2012.02.004
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1818 (5) Sequence Number: - Start / End Page: 1342 - 1350 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702