Journal of Bacteriology, August 1999, p. 5131-5133, Vol. 181, No. 16
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Biotechnology Center, Tufts University, Medford, Massachusetts 02155
Received 10 May 1999/Accepted 8 June 1999
EmrR, the repressor of the emrRAB operon of
Escherichia coli, was purified to 95% homogeneity. EmrR
was found to bind putative ligands of the EmrAB
pump
2,4-dinitrophenol, carbonyl cyanide m-chlorophenylhydrazone, and carbonyl cyanide
p-(trifluoro-methoxy)phenylhydrazone
with affinities in
the micromolar range. Equilibrium dialysis experiments suggested one
bound ligand per monomer of the dimeric EmrR.
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