Previous Article | Next Article ![]()
J Bacteriol, June 1998, p. 2817-2821, Vol. 180, No. 11
Center for Pharmaceutical Biotechnology and
Department of Medicinal Chemistry and Pharmacognosy, University of
Illinois, Chicago, Illinois 60607
Received 4 February 1998/Accepted 25 March 1998
Substitution of threonine or serine for the evolutionary conserved
intramembrane proline P347 of the Bacillus
subtilis multidrug transporter Bmr significantly increases the
toxin-effluxing activity of Bmr without affecting its abundance in the
cell. In cocultivation experiments, we demonstrate that although the
mutant T347 Bmr is advantageous to cells growing in the
presence of a toxin, the wild-type P347 Bmr is advantageous
under the conditions of nutritional limitation. This may explain why
Bmr has evolved the way it did, that is, with proline at position 347. These observations provide a basis for speculating that the evolution
of Bmr has been determined by its presently unidentified natural
function rather than by its ability to expel diverse toxins from the
cell.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Paradoxical Enhancement of the Activity of a
Bacterial Multidrug Transporter Caused by Substitutions of a
Conserved Residue
*
Corresponding author. Mailing address: Center for
Pharmaceutical Biotechnology (M/C 870), University of Illinois, 900 S. Ashland Ave., Chicago, IL 60607. Phone: (312) 996-7231. Fax: (312)
413-9303. E-mail: neyfakh{at}uic.edu.
This article has been cited by other articles:
| Appl. Environ. Microbiol. | Infect. Immun. | Eukaryot. Cell |
|---|---|---|
| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
| ALL ASM JOURNALS |