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一种保守的细胞极决定因子组织适当的极鞭毛形成。

A conserved cell-pole determinant organizes proper polar flagellum formation.

作者信息

Arroyo-Pérez Erick E, Hook John C, Alvarado Alejandra, Wimmi Stephan, Glatter Timo, Thormann Kai, Ringgaard Simon

机构信息

Max Planck Institute for Terrestrial Microbiology, Department of Ecophysiology, Munich, Germany.

Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany.

出版信息

Elife. 2024 Dec 5;13:RP93004. doi: 10.7554/eLife.93004.

DOI:10.7554/eLife.93004
PMID:39636223
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11620751/
Abstract

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 , , and , 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.

摘要

在运动性细菌中,细胞周期进程与鞭毛合成的协调是一个复杂的过程。在γ-变形杆菌中,鞭毛定位于细胞极是由SRP型GTP酶FlhF介导的。然而,FlhF的作用机制及其与细胞极标志性蛋白HubP的关系仍不清楚。在本研究中,我们发现了一种名为FipA的新蛋白,它是极性鞭毛合成中正常FlhF活性和功能所必需的。我们证明,膜定位的FipA与FlhF相互作用,在大肠杆菌、肺炎克雷伯菌和铜绿假单胞菌中是正常鞭毛合成所必需的,并且它的作用独立于由HubP介导的极性定位。FipA表现出动态定位模式,在鞭毛合成开始之前就存在于指定的极,这表明它在许可鞭毛形成中发挥作用。这一发现为调节鞭毛合成和协调依赖极性鞭毛和FlhF依赖性定位的细菌中的细胞组织的新途径提供了见解。

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