Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function

ABSTRACT Many motile bacteria swim or swarm using a filamentous rotating organelle, the flagellum. FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria. Here we determined the structure of the periplasmic region of Fl...

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Autores principales:	Norihiro Takekawa, Miyu Isumi, Hiroyuki Terashima, Shiwei Zhu, Yuuki Nishino, Mayuko Sakuma, Seiji Kojima, Michio Homma, Katsumi Imada
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2019
Materias:	bacterial flagellar motor crystal structure mechanosensor stator stomatin Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/c1cb114bdb90420d873d81dea5accb51
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spelling	oai:doaj.org-article:c1cb114bdb90420d873d81dea5accb512021-11-15T15:55:25ZStructure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function10.1128/mBio.00292-192150-7511https://doaj.org/article/c1cb114bdb90420d873d81dea5accb512019-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00292-19https://doaj.org/toc/2150-7511ABSTRACT Many motile bacteria swim or swarm using a filamentous rotating organelle, the flagellum. FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria. Here we determined the structure of the periplasmic region of FliL (FliLPeri) of the polar flagellum of Vibrio alginolyticus. FliLPeri shows a remarkable structural similarity to the stomatin/prohibitin/flotillin/HflK/C (SPFH) domain of stomatin family proteins, some of which are involved in modulation of ion channel activities in various organisms. FliLPeri forms a ring assembly in the crystal with an inner diameter of around 8 nm, which is comparable to the size of the stator unit. Mutational analyses suggest that the FliL ring forms a complex with the stator unit and that the length of the periplasmic linkers of FliL and the stator B-subunit is essential for the complex formation. We propose a model of the FliL-stator complex to discuss how Vibrio FliL modulates stator function in the bacterial flagellar motor under conditions of high viscosity. IMPORTANCE Some flagellated bacteria regulate motor torque in response to the external load change. This behavior is critical for survival, but the mechanism has remained unknown. Here, we focused on a key protein, FliL of Vibrio alginolyticus, and solved the crystal structure of its periplasmic region (FliLPeri). FliLPeri reveals striking structural similarity to a conserved domain of stomatin, which is involved in ion channel regulation in some organisms, including mammals. FliLPeri forms a ring with an inner diameter that is comparable in size to the stator unit. The mutational analyses suggested that the presence of the ring-like assembly of FliL around the stator unit enhances the surface swarming of Vibrio cells. Our study data also imply that the structural element for the ion channel regulation is conserved from bacteria to mammals.Norihiro TakekawaMiyu IsumiHiroyuki TerashimaShiwei ZhuYuuki NishinoMayuko SakumaSeiji KojimaMichio HommaKatsumi ImadaAmerican Society for Microbiologyarticlebacterial flagellar motorcrystal structuremechanosensorstatorstomatinMicrobiologyQR1-502ENmBio, Vol 10, Iss 2 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	bacterial flagellar motor crystal structure mechanosensor stator stomatin Microbiology QR1-502
spellingShingle	bacterial flagellar motor crystal structure mechanosensor stator stomatin Microbiology QR1-502 Norihiro Takekawa Miyu Isumi Hiroyuki Terashima Shiwei Zhu Yuuki Nishino Mayuko Sakuma Seiji Kojima Michio Homma Katsumi Imada Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function
description	ABSTRACT Many motile bacteria swim or swarm using a filamentous rotating organelle, the flagellum. FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria. Here we determined the structure of the periplasmic region of FliL (FliLPeri) of the polar flagellum of Vibrio alginolyticus. FliLPeri shows a remarkable structural similarity to the stomatin/prohibitin/flotillin/HflK/C (SPFH) domain of stomatin family proteins, some of which are involved in modulation of ion channel activities in various organisms. FliLPeri forms a ring assembly in the crystal with an inner diameter of around 8 nm, which is comparable to the size of the stator unit. Mutational analyses suggest that the FliL ring forms a complex with the stator unit and that the length of the periplasmic linkers of FliL and the stator B-subunit is essential for the complex formation. We propose a model of the FliL-stator complex to discuss how Vibrio FliL modulates stator function in the bacterial flagellar motor under conditions of high viscosity. IMPORTANCE Some flagellated bacteria regulate motor torque in response to the external load change. This behavior is critical for survival, but the mechanism has remained unknown. Here, we focused on a key protein, FliL of Vibrio alginolyticus, and solved the crystal structure of its periplasmic region (FliLPeri). FliLPeri reveals striking structural similarity to a conserved domain of stomatin, which is involved in ion channel regulation in some organisms, including mammals. FliLPeri forms a ring with an inner diameter that is comparable in size to the stator unit. The mutational analyses suggested that the presence of the ring-like assembly of FliL around the stator unit enhances the surface swarming of Vibrio cells. Our study data also imply that the structural element for the ion channel regulation is conserved from bacteria to mammals.
format	article
author	Norihiro Takekawa Miyu Isumi Hiroyuki Terashima Shiwei Zhu Yuuki Nishino Mayuko Sakuma Seiji Kojima Michio Homma Katsumi Imada
author_facet	Norihiro Takekawa Miyu Isumi Hiroyuki Terashima Shiwei Zhu Yuuki Nishino Mayuko Sakuma Seiji Kojima Michio Homma Katsumi Imada
author_sort	Norihiro Takekawa
title	Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function
title_short	Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function
title_full	Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function
title_fullStr	Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function
title_full_unstemmed	Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function
title_sort	structure of <italic toggle="yes">vibrio</italic> flil, a new stomatin-like protein that assists the bacterial flagellar motor function
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/c1cb114bdb90420d873d81dea5accb51
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Structure of <italic toggle="yes">Vibrio</italic> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function

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