Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in <i>Campylobacter jejuni</i>

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 <i>Campylobacter jejuni</i>. 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 <i>Campylobacterota</i>. 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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Publication Details

Journal
Proceedings of the National Academy of Sciences
Published
2024-12-30
DOI
https://doi.org/10.1073/pnas.2412594121
Citations
5
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
2.75

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article

Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni

Shoichi Tachiyama, Hang Zhao, Yuanyuan Chen, Yuqian Li et al.
5 citations
Proceedings of the National Academy of Sciences
Bacterial Genetics and Biotechnology
2.75
article

Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni

Shoichi Tachiyama, Hang Zhao, Yuanyuan Chen, Yuqian Li, Canfeng Hua, María Lara‐Tejero, Beile Gao, Jun Liu, Yuming Guo, Yanmin Wu, Xueyin Feng
article en
5 citations

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 <i>Campylobacter jejuni</i>. 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 <i>Campylobacterota</i>. 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.

Proceedings of the National Academy of SciencesVol. 122(1)
Henan University (CN), Chinese Academy of Sciences (CN), Yale University (US), Institute of Oceanology (CN), South China Sea Institute Of Oceanology (CN), Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou) (CN), University of Chinese Academy of Sciences (CN)
Yale University, National Natural Science Foundation of China, Chinese Academy of Sciences, Henan University, South China University of Technology, Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou), National Institutes of Health, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Institute of Oceanology, Chinese Academy of Sciences, National Key Research and Development Program of China, Science and Technology Planning Project of Guangdong Province, National Institute of Allergy and Infectious Diseases
Openalex Percentile: Top 9%
Bacterial Genetics and Biotechnology
2.75
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