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Journal of Bacteriology, August 2006, p. 5635-5639, Vol. 188, No. 15
0021-9193/06/$08.00+0     doi:10.1128/JB.00422-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

No Single Irreplaceable Acidic Residues in the Escherichia coli Secondary Multidrug Transporter MdfA

Nadejda Sigal, Shahar Molshanski-Mor, and Eitan Bibi*

Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel

Received 27 March 2006/ Accepted 11 May 2006

The largest family of solute transporters (major facilitator superfamily [MFS]) includes proton-motive-force-driven secondary transporters. Several characterized MFS transporters utilize essential acidic residues that play a critical role in the energy-coupling mechanism during transport. Surprisingly, we show here that no single acidic residue plays an irreplaceable role in the Escherichia coli secondary multidrug transporter MdfA.

* Corresponding author. Mailing address: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. Phone: 972-8-9343464. Fax: 972-8-9344118. E-mail: e.bibi{at}weizmann.ac.il.

Journal of Bacteriology, August 2006, p. 5635-5639, Vol. 188, No. 15
0021-9193/06/$08.00+0     doi:10.1128/JB.00422-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sigal, N., Fluman, N., Siemion, S., Bibi, E. (2009). The Secondary Multidrug/Proton Antiporter MdfA Tolerates Displacements of an Essential Negatively Charged Side Chain. J. Biol. Chem. 284: 6966-6971 [Abstract] [Full Text]  
  • Pasrija, R., Banerjee, D., Prasad, R. (2007). Structure and Function Analysis of CaMdr1p, a Major Facilitator Superfamily Antifungal Efflux Transporter Protein of Candida albicans: Identification of Amino Acid Residues Critical for Drug/H+ Transport. Eukaryot Cell 6: 443-453 [Abstract] [Full Text]  


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