His257 is a uniquely important histidine residue for tetracycline/H+ antiport function but not mandatory for full activity of the transposon Tn10-encoded metal-tetracycline/H+ antiporter

Biochemistry
A YamaguchiT Sawai

Abstract

His257 is the only histidine residue located in the putative transmembrane region of the Tn10-encoded metal-tetracycline/H+ antiporter (TetA) and contributes to the substrate/H+ coupling [Yamaguchi, A.. Adachi, K., Akasaka. T., Ono. N., & Sawai, T. (1991) J. Biol. Chem. 266, 6045-6051]. Tn10-TetA contains five histidine residues, including His257. When these histidine residues were replaced by alanine one by one, only the His257Ala mutant showed almost complete loss of the tetracycline transport activity, whereas the other four His --> Ala mutants, H42A, H158A, H329A, and H359A, retained transport activity comparable to that of the wild type. The mutant which contains only one histidine, His257, retained about 80% of the wild-type activity, whereas the histidine-less mutant, in which all five histidine residues were replaced by Ala, exhibited little activity. These results clearly indicated that His257 is a unique histidine residue in TetA responsible for the transport activity. The His257Tyr mutant, irrespective of the presence or absence of the other four histidine residues, retained about 30% of the wild-type tetracycline transport activity and showed corresponding tetracycline-coupled H+ translocation, indicating that an im...Continue Reading

Citations

Oct 29, 2003·Current Opinion in Chemical Biology·Norihisa TamuraAkihito Yamaguchi
Jun 21, 2001·The Biochemical Journal·C A WiebeL Fliegel
Oct 29, 2009·Cellular and Molecular Life Sciences : CMLS·Maulik ThakerGerard D Wright
Apr 9, 2008·Journal of Molecular Biology·Christopher J LawDa-Neng Wang
May 28, 2003·Biochemical and Biophysical Research Communications·G Shane LewisKurt W Miller
Sep 21, 2005·The Journal of Antimicrobial Chemotherapy·Maria SangvikKristin Hegstad Dahl

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