Site-directed crosslinking identifies the stator-rotor interaction surfaces in a hybrid bacterial flagellar motor.

ABSTRACT: The bacterial flagellum is the motility organelle powered by a rotary motor. The rotor and stator elements of the motor are located in the cytoplasmic membrane and cytoplasm. The stator units assemble around the rotor, and an ion flux (typically H⁺ or Na⁺) conducted through a channel of the stator induces conformational changes that generate rotor torque. Electrostatic interactions between the stator protein PomA in Vibrio (MotA in Escherichia coli) and the rotor protein FliG have been shown by genetic analyses, but have not been demonstrated biochemically. Here, we used site-directed photo- and disulfide-crosslinking to provide direct evidence for the interaction. We introduced a UV-reactive amino acid, p-benzoyl-L-phenylalanine (pBPA), in

SUBMITTER: Terashima H 

PROVIDER: S-EPMC8092157 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature