Ligand binding specificity of RutR, a member of the TetR family of transcription regulators in Escherichia coli.

ABSTRACT: RutR is a member of the large family of TetR transcriptional regulators in Escherichia coli. It was originally discovered as the regulator of the rutABCDEFG operon encoding a novel pathway for pyrimidine utilization, but its highest affinity target is the control region of the carAB operon, encoding carbamoylphosphate synthase. Unlike most other TetR-like regulators, RutR exerts both positive and negative effects on promoter activity. Furthermore, RutR exhibits a very narrow ligand binding specificity, unlike the broad effector specificity that characterizes some of the well-studied multidrug resistance regulators of the family. Here we focus on ligand binding and ligand specificity of RutR. We construct single alanine substitution mutants of amino acid residues of the ligand-binding pocke

SUBMITTER: Nguyen Le Minh P 

PROVIDER: S-EPMC4325133 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature