PMID:10438794

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Citation

Brooun, A, Tomashek, JJ and Lewis, K (1999) Purification and ligand binding of EmrR, a regulator of a multidrug transporter. J. Bacteriol. 181:5131-3

Abstract

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.

Links

PubMed PMC94011

Keywords

2,4-Dinitrophenol/metabolism; 2,4-Dinitrophenol/pharmacology; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Binding, Competitive/drug effects; Carbonyl Cyanide m-Chlorophenyl Hydrazone/metabolism; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone/metabolism; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone/pharmacology; Dialysis; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Ligands; P-Glycoprotein/isolation & purification; P-Glycoprotein/metabolism; Repressor Proteins/genetics; Repressor Proteins/isolation & purification; Repressor Proteins/metabolism; Transcription Factors

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