Abstract
The flagellar motor rotates bi-directionally in counter-clockwise (CCW) and clockwise (CW) directions. The motor consists of a stator and a rotor. Recent structural studies have revealed that the stator is composed of a pentameric ring of A subunits and a dimer axis of B subunits. Highly conserved charged and neighboring residues of the A subunit interacts with the rotor, generating torque through a gear-like mechanism. The rotational direction is controlled by chemotaxis signaling transmitted to the rotor, with less evidence for the stator being involved. In this study, we report novel mutations that affect the switching of the rotational direction at the putative interaction site of the stator to generate rotational force. Our results highlight an aspect of flagellar motor function that appropriate switching of the interaction states between the stator and rotor is critical for controlling the rotational direction.
Highlights
The flagellar motor rotates bi-directionally in counter-clockwise (CCW) and clockwise (CW) directions
A previous report showed that F92 and L93 of PomA are located very close to the C-terminal region of FliG in the rotor and suggested that these residues are involved in the interaction between the stator and rotor in addition to conserved charged residues[7]
The rotational direction of the flagellar motor is mainly controlled by CheY-P and the C-ring proteins, FliG, FliM, and FliN
Summary
The flagellar motor rotates bi-directionally in counter-clockwise (CCW) and clockwise (CW) directions. From the structure in which two molecules of MotB are inserted in the center of the MotA five-molecule ring, a gear-like rotation model between the stator and rotor has been p roposed[5,6,7,8]. In this model, the MotA ring may rotate in CCW direction by default with respect to the axis of MotB coupled to the influx of ions through a transmembrane ion channel. This region is not directly involved in the ion conduction
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