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In Vitro Autonomous Construction of the Flagellar Axial Structure in Inverted Membrane Vesicles
Open AccessFeature PaperArticle

Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC

1
Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
2
RIKEN Center for Biosystems Dynamics Research, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
3
Faculty of Science and Engineering, Chuo University, Tokyo 112-8551, Japan
4
RIKEN SPring-8 Center, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
5
JEOL YOKOGUSHI Research Alliance Laboratories, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Current address: Thermo Fisher Scientific K.K., 4-2-8 Shibaura, Minato-ku, Tokyo 108-0023, Japan.
§
Current address: Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Biomolecules 2020, 10(2), 246; https://doi.org/10.3390/biom10020246
Received: 27 December 2019 / Revised: 28 January 2020 / Accepted: 4 February 2020 / Published: 6 February 2020
(This article belongs to the Special Issue Perspectives on Bacterial Flagellar Motor)
The bacterial flagellum is a motility organelle consisting of a long helical filament as a propeller and a rotary motor that drives rapid filament rotation to produce thrust. Salmonella enterica serovar Typhimurium has two genes of flagellin, fljB and fliC, for flagellar filament formation and autonomously switches their expression at a frequency of 10−3–10−4 per cell per generation. We report here differences in their structures and motility functions under high-viscosity conditions. A Salmonella strain expressing FljB showed a higher motility than one expressing FliC under high viscosity. To examine the reasons for this motility difference, we carried out structural analyses of the FljB filament by electron cryomicroscopy and found that the structure was nearly identical to that of the FliC filament except for the position and orientation of the outermost domain D3 of flagellin. The density of domain D3 was much lower in FljB than FliC, suggesting that domain D3 of FljB is more flexible and mobile than that of FliC. These differences suggest that domain D3 plays an important role not only in changing antigenicity of the filament but also in optimizing motility function of the filament as a propeller under different conditions. View Full-Text
Keywords: bacterial flagellar motility; flagellin; Salmonella; FljB; FliC; electron cryomicroscopy; viscosity; infection bacterial flagellar motility; flagellin; Salmonella; FljB; FliC; electron cryomicroscopy; viscosity; infection
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Yamaguchi, T.; Toma, S.; Terahara, N.; Miyata, T.; Ashihara, M.; Minamino, T.; Namba, K.; Kato, T. Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC. Biomolecules 2020, 10, 246.

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