The drug-binding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain.
نویسندگان
چکیده
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.
منابع مشابه
Structural Basis of Multidrug Recognition by BmrR, a Transcription Activator of a Multidrug Transporter
Multidrug-efflux transporters demonstrate an unusual ability to recognize multiple structurally dissimilar toxins. A comparable ability to bind diverse hydrophobic cationic drugs is characteristic of the Bacillus subtilis transcription regulator BmrR, which upon drug binding activates expression of the multidrug transporter Bmr. Crystal structures of the multidrug-binding domain of BmrR (2.7 A ...
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عنوان ژورنال:
- Journal of bacteriology
دوره 178 5 شماره
صفحات -
تاریخ انتشار 1996