School of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul, 08826, Republic of Korea.
Department of Biophysics and Chemical Biology, Seoul National University, Seoul, 08826, Republic of Korea.
Mol Microbiol. 2019 Jul;112(1):266-279. doi: 10.1111/mmi.14268. Epub 2019 May 18.
How motile bacteria recognize their environment and decide whether to stay or navigate toward more favorable location is a fundamental issue in survival. The flagellum is an elaborate molecular device responsible for bacterial locomotion, and the flagellum-driven motility allows bacteria to move themselves to the appropriate location at the right time. Here, we identify the polar landmark protein HubP as a modulator of polar flagellation that recruits the flagellar assembly protein FapA to the old cell pole, thereby controlling its activity for the early events of flagellar assembly in Vibrio vulnificus. We show that dephosphorylated EIIA of the PEP-dependent sugar transporting phosphotransferase system sequesters FapA from HubP in response to glucose and hence inhibits FapA-mediated flagellation. Thus, flagellar assembly and motility is governed by spatiotemporal control of FapA, which is orchestrated by the competition between dephosphorylated EIIA and HubP, in the human pathogen V. vulnificus.
运动细菌如何识别环境并决定是停留还是朝着更有利的位置移动，这是生存的一个基本问题。鞭毛是一种负责细菌运动的精细分子装置，鞭毛驱动的运动使细菌能够在适当的时间移动到适当的位置。在这里，我们将极性地标蛋白 HubP 鉴定为极性鞭毛的调节剂，它将鞭毛组装蛋白 FapA 招募到旧的细胞极，从而控制其在弧菌鞭毛组装的早期事件中的活性。我们表明，PEP 依赖性糖转运磷酸转移酶系统的去磷酸化 EIIA 响应葡萄糖将 FapA 从 HubP 隔离出来，从而抑制 FapA 介导的鞭毛形成。因此，在人类病原体弧菌中，鞭毛的组装和运动受 FapA 的时空控制，这是由去磷酸化的 EIIA 和 HubP 之间的竞争来协调的。
