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Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC
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 auton...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7072241/ https://www.ncbi.nlm.nih.gov/pubmed/32041169 http://dx.doi.org/10.3390/biom10020246 |
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author | Yamaguchi, Tomoko Toma, Shoko Terahara, Naoya Miyata, Tomoko Ashihara, Masamichi Minamino, Tohru Namba, Keiichi Kato, Takayuki |
author_facet | Yamaguchi, Tomoko Toma, Shoko Terahara, Naoya Miyata, Tomoko Ashihara, Masamichi Minamino, Tohru Namba, Keiichi Kato, Takayuki |
author_sort | Yamaguchi, Tomoko |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7072241 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-70722412020-03-19 Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC Yamaguchi, Tomoko Toma, Shoko Terahara, Naoya Miyata, Tomoko Ashihara, Masamichi Minamino, Tohru Namba, Keiichi Kato, Takayuki Biomolecules Article 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. MDPI 2020-02-06 /pmc/articles/PMC7072241/ /pubmed/32041169 http://dx.doi.org/10.3390/biom10020246 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Yamaguchi, Tomoko Toma, Shoko Terahara, Naoya Miyata, Tomoko Ashihara, Masamichi Minamino, Tohru Namba, Keiichi Kato, Takayuki Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC |
title | Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC |
title_full | Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC |
title_fullStr | Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC |
title_full_unstemmed | Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC |
title_short | Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC |
title_sort | structural and functional comparison of salmonella flagellar filaments composed of fljb and flic |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7072241/ https://www.ncbi.nlm.nih.gov/pubmed/32041169 http://dx.doi.org/10.3390/biom10020246 |
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