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Stoichiometry of Metal-tetracycline/H+ Antiport Mediated by Transposon Tn10-encoded Tetracycline Resistance Protein in Escherichia Coli

Overview
Journal FEBS Lett
Specialty Biochemistry
Date 1991 May 6
PMID 1645287
Citations 20
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Abstract

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.

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