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Journal of Bacteriology, March 2002, p. 1796-1800, Vol. 184, No. 6
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.6.1796-1800.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Site-Directed Mutagenesis Studies of Selected Motif and Charged Residues and of Cysteines of the Multifunctional Tetracycline Efflux Protein Tet(L)

Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, New York, New York 10029

Received 12 October 2001/ Accepted 18 December 2001

All of the transmembrane glutamates of Tet(L) are essential for tetracycline (TET) resistance, and E397 has been shown to be essential for all catalytic modes, i.e., TET-Me²⁺ and Na⁺ efflux and K⁺ uptake. Loop residues D74 and G70 are essential for TET flux but not for Na⁺ or K⁺ flux. A cysteineless Tet(L) protein exhibits all activities.

This article has been cited by other articles:

• 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]