Na⁺-induced structural transition of MotPS for stator assembly of the Bacillus flagellar motor.

ABSTRACT: The bacterial flagellar motor consists of a rotor and a dozen stator units and regulates the number of active stator units around the rotor in response to changes in the environment. The MotPS complex is a Na⁺-type stator unit in the Bacillus subtilis flagellar motor and binds to the peptidoglycan layer through the peptidoglycan-binding (PGB) domain of MotS to act as the stator. The MotPS complex is activated in response to an increase in the Na⁺ concentration in the environment, but the mechanism of this activation has remained unknown. We report that activation occurs by a Na⁺-induced folding and dimer formation of the PGB domain of MotS, as revealed in real-time imaging by high-speed atomic force microscopy. The MotPS complex showed two distinct e

SUBMITTER: Terahara N 

PROVIDER: S-EPMC5665596 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature