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Polar landmark protein HubP recruits flagella assembly protein FapA under glucose limitation in Vibrio vulnificus

Cited 12 time in Web of Science Cited 12 time in Scopus
Authors

Park, Soyoung; Yoon, Jihee; Lee, Chang-Ro; Lee, Ju Yeon; Kim, Yeon-Ran; Jang, Kyoung-Soon; Lee, Kyu-Ho; Seok, Yeong-Jae

Issue Date
2019-07
Publisher
Blackwell Publishing Inc.
Citation
Molecular Microbiology, Vol.112 No.1, pp.266-279
Abstract
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.
ISSN
0950-382X
URI
https://hdl.handle.net/10371/192878
DOI
https://doi.org/10.1111/mmi.14268
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