FliL association with flagellar stator in the sodium-driven Vibrio motor characterized by the fluorescent microscopy

Tsai Shun Lin, Shiwei Zhu, Seiji Kojima, Michio Homma, Chien Jung Lo

研究成果: 雜誌貢獻期刊論文同行評審

16 引文 斯高帕斯(Scopus)

摘要

Bacterial flagellar motor (BFM) is a protein complex used for bacterial motility and chemotaxis that involves in energy transformation, torque generation and switching. FliL is a single-transmembrane protein associated with flagellar motor function. We performed biochemical and biophysical approaches to investigate the functional roles of FliL associated with stator-units. Firstly, we found the periplasmic region of FliL is crucial for its polar localization. Also, the plug mutation in stator-unit affected the polar localization of FliL implying the activation of stator-unit is important for FliL recruitment. Secondly, we applied single-molecule fluorescent microscopy to study the role of FliL in stator-unit assembly. Using molecular counting by photobleaching, we found the stoichiometry of stator-unit and FliL protein would be 1:1 in a functional motor. Moreover, the turnover time of stator-units are slightly increased in the absence of FliL. By further investigation of protein dynamics on membrane, we found the diffusions of stator-units and FliL are independent. Surprisingly, the FliL diffusion rate without stator-units is unexpectedly slow indicating a protein-complex forming event. Our results suggest that FliL plays a supporting role to the stator in the BFM.

原文???core.languages.en_GB???
文章編號11172
期刊Scientific Reports
8
發行號1
DOIs
出版狀態已出版 - 1 12月 2018

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