The single polar flagellum of Shewanella oneidensis MR-1 is powered by two different stator complexes, the sodium-dependent PomAB and the proton-driven MotAB. In addition, Shewanella harbors two genes with homology to motX and motY of Vibrio species. In Vibrio, the products of these genes are crucial for sodium-dependent flagellar rotation. Resequencing of S. oneidensis MR-1 motY revealed that the gene does not harbor an authentic frameshift as was originally reported. Mutational analysis demonstrated that both MotX and MotY are critical for flagellar rotation of S. oneidensis MR-1 for both sodium- and proton-dependent stator systems but do not affect assembly of the flagellar filament. Fluorescence tagging of MotX and MotY to mCherry revealed that both proteins localize to the flagellated cell pole depending on the presence of the basal flagellar structure. Functional localization of MotX requires MotY, whereas MotY localizes independently of MotX. In contrast to the case in Vibrio, neither protein is crucial for the recruitment of the PomAB or MotAB stator complexes to the flagellated cell pole, nor do they play a major role in the stator selection process. Thus, MotX and MotY are not exclusive features of sodium-dependent flagellar systems. Furthermore, MotX and MotY in Shewanella, and possibly also in other genera, must have functions beyond the recruitment of the stator complexes.
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http://dx.doi.org/10.1128/JB.00206-09 | DOI Listing |
Front Microbiol
April 2022
Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
The bacterial flagellar stator is a unique ion-conducting membrane protein complex composed of two kinds of proteins, the A subunit and the B subunit. The stator couples the ion-motive force across the membrane into rotational force. The stator becomes active only when it is incorporated into the flagellar motor.
View Article and Find Full Text PDFJ Bacteriol
January 2020
Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, USA
The bacterial flagellum is a biological nanomachine that rotates to allow bacteria to swim. For flagellar rotation, torque is generated by interactions between a rotor and a stator. The stator, which is composed of MotA and MotB subunit proteins in the membrane, is thought to bind to the peptidoglycan (PG) layer, which anchors the stator around the rotor.
View Article and Find Full Text PDFMethods Mol Biol
February 2018
Division of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan.
Most bacteria can swim by rotating the flagellum. The basal body of the flagellum is an essential part for this motor function. Recent comprehensive analysis of the flagellar basal body structures across bacteria by cryo-electron tomography has revealed that they all share core structures, the rod, and rings: the C ring, M ring, S ring, L ring, and P ring.
View Article and Find Full Text PDFJ Biochem
February 2017
Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
The bacterial flagellar motor is a rotary motor complex composed of various proteins. The motor contains a central rod, multiple ring-like structures and stators. The Na+-driven polar flagellar motor of the marine bacterium Vibrio alginolyticus has a specific ring, called the ‘T-ring’, which consists of two periplasmic proteins, MotX and MotY.
View Article and Find Full Text PDFFront Microbiol
August 2016
Departamento de Genética, Microbiología y Estadística, Sección Microbiologia, Virología y Biotecnología, Facultad de Biología, Universidad de Barcelona Barcelona, Spain.
Aeromonas hydrophila sodium-driven polar flagellum has a complex stator-motor. Consist of two sets of redundant and non-exchangeable proteins (PomA/PomB and PomA2/PomB2), which are homologs to other sodium-conducting polar flagellum stator motors; and also two essential proteins (MotX and MotY), that they interact with one of those two redundant pairs of proteins and form the T-ring. In this work, we described an essential protein for polar flagellum stability and rotation which is orthologs to Vibrio spp.
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