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J. Biol. Chem., Vol. 265, Issue 26, 15525-15530, 09, 1990
A Yamaguchi, N Ono, T Akasaka, T Noumi and T Sawai
The transposon Tn10-encoded tetracycline resistance protein functions as a
metal-tetracycline/H+ antiporter (Yamaguchi, A., Udagawa, T., and Sawai, T.
(1990) J. Biol. Chem. 265, 4809-4813). The Ser65-Asp66 dipeptide is
conserved in all known tetracycline antiporter proteins and is an important
target for site-directed mutagenesis. When Asp66 was replaced by Asn, the
transport activity was completely lost, whereas when it was replaced by
Glu, the activity was reduced to 10% of the wild-type level, indicating
that a negative charge at position 66 is essential for tetracycline
transport. Replacement of Ser65 by Cys or Ala, in contrast, caused only a
minor change in tetracycline transport activity. However, the Cys65 mutant
antiporter was sensitive to sulfhydryl reagents. Complete inactivation of
the Cys65 antiporter by N- ethylmaleimide was not prevented by the
substrate. A less bulky reagent, methyl methanethiosulfonate, caused
partial inactivation of the Cys65 antiporter without changing its affinity
to the substrate. These results indicate that a region including the
dipeptide plays an important role in metal-tetracycline transport except
for substrate binding. It may act as a gate which opens on the
charge-charge interaction between Asp66 and the metal-tetracycline.
Metal-tetracycline/H+ antiporter of Escherichia coli encoded by a transposon, Tn10. The role of the conserved dipeptide, Ser65-Asp66, in tetracycline transport
Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, Japan.
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