globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1712489114
论文题名:
Molecular architecture of the sheathed polar flagellum in Vibrio alginolyticus
作者: Zhu S.; Nishikino T.; Hu B.; Kojima S.; Homma M.; Liu J.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2017
卷: 114, 期:41
起始页码: 10966
结束页码: 10971
语种: 英语
英文关键词: Electron tomography ; Flagellum ; Nanomachine ; Vibrio
Scopus关键词: amino terminal sequence ; Article ; bacterial cell ; carboxy terminal sequence ; cell membrane ; cell motility ; conformational transition ; controlled study ; electron tomography ; Escherichia coli ; flagellum ; high throughput screening ; inner membrane ; molecular dynamics ; nonhuman ; outer membrane ; priority journal ; structure analysis ; Vibrio alginolyticus ; cytology ; flagellum ; genetics ; metabolism ; procedures ; ultrastructure ; Vibrio alginolyticus ; bacterial protein ; sodium ; Bacterial Proteins ; Electron Microscope Tomography ; Flagella ; Sodium ; Vibrio alginolyticus
英文摘要: Vibrio species are Gram-negative rod-shaped bacteria that are ubiquitous and often highly motile in aqueous environments. Vibrio swimming motility is driven by a polar flagellum covered with a membranous sheath, but this sheathed flagellum is not well understood at the molecular level because of limited structural information. Here, we use Vibrio alginolyticus as a model system to study the sheathed flagellum in intact cells by combining cryoelectron tomography (cryo-ET) and subtomogram analysis with a genetic approach. We reveal striking differences between sheathed and unsheathed flagella in V. alginolyticus cells, including a novel ring-like structure at the bottom of the hook that is associated with major remodeling of the outer membrane and sheath formation. Using mutants defective in flagellar motor components, we defined a Vibrio-specific feature (also known as the T ring) as a distinctive periplasmic structure with 13-fold symmetry. The unique architecture of the T ring provides a static platform to recruit the PomA/B complexes, which are required to generate higher torques for rotation of the sheathed flagellum and fast motility of Vibrio cells. Furthermore, the Vibrio flagellar motor exhibits an intrinsic length variation between the inner and the outer membrane bound complexes, suggesting the outer membrane bound complex can shift slightly along the axial rod during flagellar rotation. Together, our detailed analyses of the polar flagella in intact cells provide insights into unique aspects of the sheathed flagellum and the distinct motility of Vibrio species. © 2017, National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163788
Appears in Collections:气候变化与战略

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作者单位: Zhu, S., Department of Pathology and Laboratory Medicine, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX 77030, United States, Department of Microbial Pathogenesis, Microbial Sciences Institute, Yale School of Medicine, New Haven, CT 06536, United States; Nishikino, T., Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya, 464-8602, Japan; Hu, B., Department of Pathology and Laboratory Medicine, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX 77030, United States; Kojima, S., Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya, 464-8602, Japan; Homma, M., Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya, 464-8602, Japan; Liu, J., Department of Pathology and Laboratory Medicine, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX 77030, United States, Department of Microbial Pathogenesis, Microbial Sciences Institute, Yale School of Medicine, New Haven, CT 06536, United States

Recommended Citation:
Zhu S.,Nishikino T.,Hu B.,et al. Molecular architecture of the sheathed polar flagellum in Vibrio alginolyticus[J]. Proceedings of the National Academy of Sciences of the United States of America,2017-01-01,114(41)
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