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Mol Microbiol. 2019 May 6. doi: 10.1111/mmi.14268. [Epub ahead of print]

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

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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.
Department of Biological Sciences, Myongji University, Yongin, 17058, Republic of Korea.
Biomedical Omics Group, Korea Basic Science Institute, Cheongju, 28119, Republic of Korea.
Department of Biological Sciences, Sogang University, Seoul, 04107, Republic of Korea.


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 EIIAGlc 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 EIIAGlc and HubP, in the human pathogen V. vulnificus.


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