TY - JOUR AU - Tetsch, Larissa AU - Koller, Christiane AU - Dönhöfer, Alexandra AU - Jung, Kirsten PY - 2011 DA - 2011/04/12 TI - Detection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli JO - BMC Microbiology SP - 74 VL - 11 IS - 1 AB - In an acidic and lysine-rich environment Escherichia coli induces expression of the cadBA operon which encodes CadA, the lysine decarboxylase, and CadB, the lysine/cadaverine antiporter. cadBA expression is dependent on CadC, a membrane-integrated transcriptional activator which belongs to the ToxR-like protein family. Activation of CadC requires two stimuli, lysine and low pH. Whereas lysine is detected by an interplay between CadC and the lysine-specific transporter LysP, pH alterations are sensed by CadC directly. Crystal structural analyses revealed a close proximity between two periplasmic cysteines, Cys208 and Cys272. SN - 1471-2180 UR - https://doi.org/10.1186/1471-2180-11-74 DO - 10.1186/1471-2180-11-74 ID - Tetsch2011 ER -