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Polar landmark protein HubP recruits flagella assembly protein FapA under glucose limitation in Vibrio vulnificus
Author(s) -
Park Soyoung,
Yoon Jihee,
Lee ChangRo,
Lee Ju Yeon,
Kim YeonRan,
Jang KyoungSoon,
Lee KyuHo,
Seok YeongJae
Publication year - 2019
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.14268
Subject(s) - flagellum , biology , vibrio vulnificus , motility , microbiology and biotechnology , bacteria , genetics
Summary 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 Glc 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 Glc and HubP, in the human pathogen V. vulnificus .