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Updated: Jun 3, 2025

Biophysical Characterization of Flagellar Motor Functions
Published on: January 18, 2017
Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in
Yuanyuan Chen1,2,3,4, Shoichi Tachiyama5,6, Yuqian Li1,2,3
1Chinese Academy of Sciences Key Laboratory of Tropical Marine Bio Resources and Ecology, Guangdong Key Laboratory of Marine Materia Medica, Innovation Academy of South China Sea Ecology and Environmental Engineering, Guangdong Provincial Observation and Research Station for Coastal Upwelling Ecosystem, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 511458, China.
Abstract:
Rotation of the bacterial flagellum, the first identified biological rotary machine, is driven by its stator units. Knowledge gained about the function of stator units has increasingly led to studies of rotary complexes in different cellular pathways. Here, we report that a tetrameric PilZ family protein, FlgX, is a structural component underneath the stator units in the flagellar motor of Campylobacter jejuni. FlgX forms a stable tetramer that does not bind cyclic di-GMP (c-di-GMP), unlike other canonical PilZ domain-containing proteins. Cryoelectron tomography and subtomogram averaging of flagellar motors in situ provide evidence that FlgX interacts with each stator unit and plays a critical role in stator ring assembly and stability. Furthermore, FlgX is conserved and was most likely present in the common ancestor of the phylum Campylobacterota. Overall, FlgX represents a divergence in function for PilZ superfamily proteins as well as a player in the key stator-rotor interaction of complex flagellar motors.
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