
FipA是一種新的FlhF互作蛋白,在細菌極性鞭毛形成中扮演重要角色。FipA與FlhF的相互作用有助於將FlhF定位到細胞極性,並促進鞭毛的合成。


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The coordination of cell cycle progression and flagellar synthesis is a complex process in motile bacteria. In γ-proteobacteria, the localization of the flagellum to the cell pole is mediated by the SRP-type GTPase FlhF. However, the mechanism of action of FlhF, and its relationship with the cell pole landmark protein HubP remain unclear. In this study, we discovered a novel protein called FipA that is required for normal FlhF activity and function in polar flagellar synthesis. We demonstrated that membrane-localized FipA interacts with FlhF and is required for normal flagellar synthesis in Vibrio parahaemolyticus , Pseudomonas putida , and Shewanella putrefaciens , and it does so independently of the polar localization mediated by HubP. FipA exhibits a dynamic localization pattern and is present at the designated pole before flagellar synthesis begins, suggesting its role in licensing flagellar formation. This discovery provides insight into a new pathway for regulating flagellum synthesis and coordinating cellular organization in bacteria that rely on polar flagellation and FlhF-dependent localization.

### Competing Interest Statement

The authors have declared no competing interest.

A conserved cell-pole determinant organizes proper polar flagellum formation

保護細胞極性決定因子組織適當的極性鞭毛形成