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Journal of Bacteriology, January 2003, p. 374-376, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.374-376.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Membrane Topology of the ZntB Efflux System of Salmonella enterica Serovar Typhimurium

Andreia M. Caldwell and Ronald L. Smith*

Department of Biology, University of Texas at Arlington, Arlington, Texas 76019

Received 1 August 2002/ Accepted 27 September 2002

The membrane topology of the ZntB Zn2+ transport protein of Salmonella enterica serovar Typhimurium was determined by constructing deletion derivatives of the protein and genetically fusing them to blaM or lacZ cassettes. The enzymatic activities of the hybrid proteins indicate that ZntB is a bitopic integral membrane protein consisting largely of two independent domains. The first 266 amino acids form a large, highly charged domain within the cytoplasm, while the remaining 61 residues form a small membrane domain containing two membrane-spanning segments. The overall orientation towards the cytoplasm is consistent with the ability of ZntB to facilitate zinc efflux.

* Corresponding author. Mailing address: Department of Biology, The University of Texas at Arlington, 501 S. Nedderman Dr., Arlington, TX 76019. Phone: (817) 272-2411. Fax: (817) 272-2855. E-mail: rlsmith{at}airmail.net.

Journal of Bacteriology, January 2003, p. 374-376, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.374-376.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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