Stoichiometry of metal-tetracycline/H+ antiport mediated by transposon Tn10-encoded tetracycline resistance protein in Escherichia coli.
The tetracycline resistance protein (TetA) endoded by transposon Tn10 mediates the efflux of divalent cation-tetracycline chelating complexes [Yamaguchi, A., Udagawa, T. and Sawai, T. (1990) J. Biol. Chem. 265, 4809-4813]. It was confirmed that protons were antiported with the complexes through an electrically-neutral process because the antiport consumed delta pH but not delta psi. The quantitative relationship between delta pH and delta pTC determined by a flow-dialysis method clearly indicated a 1:1 stoichiometry of the monocationic metal-tetracycline/H+ exchange.
Yamaguchi
A
A
Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, Japan.
Iwasaki-Ohba
Y
Y
Ono
N
N
Kaneko-Ohdera
M
M
Sawai
T
T
D002474:Cell-Free System; D004251:DNA Transposable Elements; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008564:Membrane Potentials; D013752:Tetracycline / Q000378:metabolism*; D013753:Tetracycline Resistance; D013816:Thermodynamics
D004251:DNA Transposable Elements; D013752:Tetracycline