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Journal of Bacteriology, April 2001, p. 2667-2671, Vol. 183, No. 8
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.8.2667-2671.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Twelve-Transmembrane-Segment (TMS) Version (Delta TMS VII-VIII) of the 14-TMS Tet(L) Antibiotic Resistance Protein Retains Monovalent Cation Transport Modes but Lacks Tetracycline Efflux Capacity

Jie Jin, Arthur A. Guffanti, Catherine Beck, and Terry A. Krulwich*

Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029

Received 22 November 2000/Accepted 26 January 2001

A "Tet(L)-12" version of Tet(L), a tetracycline efflux protein with 14 transmembrane segments (TMS), was constructed by deletion of two central TMS. Tet(L)-12 catalyzed Na+/H+ antiport and antiport with K+ as a coupling ion as well as or better than wild-type Tet(L) but exhibited no tetracycline-Me2+/H+ antiport in Escherichia coli vesicles.

* Corresponding author. Mailing address: Box 1020, Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029. Phone: (212) 241-7280. Fax: (212) 996-7214. E-mail: terry.krulwich{at}mssm.edu.

Journal of Bacteriology, April 2001, p. 2667-2671, Vol. 183, No. 8
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.8.2667-2671.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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  • Jin, J., Guffanti, A. A., Bechhofer, D. H., Krulwich, T. A. (2002). Tet(L) and Tet(K) Tetracycline-Divalent Metal/H+ Antiporters: Characterization of Multiple Catalytic Modes and a Mutagenesis Approach to Differences in Their Efflux Substrate and Coupling Ion Preferences. J. Bacteriol. 184: 4722-4732 [Abstract] [Full Text]  
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