The drug-binding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain.
Rhodamine and tetraphenylphosphonium, the substrates of the Bacillus subtilis multidrug efflux transporter Bmr, induce the expression of Bmr through direct interaction with its transcriptional activator BmrR. Here we show that the C-terminal domain of BmrR, expressed individually, binds both these compounds and therefore can be used as a model for molecular analysis of the phenomenon of multidrug recognition.
Markham
P N
PN
Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago 60612, USA.
Ahmed
M
M
Neyfakh
A A
AA
D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000096:biosynthesis; D026901:Membrane Transport Proteins; D009861:Onium Compounds / Q000378:metabolism*; D009943:Organophosphorus Compounds / Q000378:metabolism*; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D012235:Rhodamines / Q000378:metabolism; D013329:Structure-Activity Relationship; D015534:Trans-Activators / Q000378:metabolism*
D001426:Bacterial Proteins; C098722:BmrR protein, bacteria; D002352:Carrier Proteins; D026901:Membrane Transport Proteins; D009861:Onium Compounds; D009943:Organophosphorus Compounds; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012235:Rhodamines; D015534:Trans-Activators; C026188:rhodamine 6G; C075041:Bmr protein, Bacillus subtilis; C013289:tetraphenylphosphonium