Structural analysis of S-ring composed of FliFG fusion proteins in marine                     Vibrio                     polar flagellar motor

Takekawa, Norihiro; Nishikino, Tatsuro; Kishikawa, Junichi; Hirose, Mika; Kinoshita, Miki; Kojima, Seiji; Minamino, Tohru; Uchihashi, Takayuki; Kato, Takayuki; Imada, Katsumi; Homma, Michio

doi:https://doi.org/10.1128/mbio.01261-24

Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor

Takekawa, Norihiro; Nishikino, Tatsuro; Kishikawa, Junichi et al.

mBio, 2024, 15(10), e01261-24

Number of Access:1,421（2025-11-27 00:45 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/98250

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Title	Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor
Creator	NRID 1000050791810 1000050791810 researchmap permalink takekawan takekawan Scopus Author ID 54416513800 54416513800 CreatorName Takekawa, Norihiro
	ORCID 0000-0001-9950-3086 0000-0001-9950-3086 CreatorName Nishikino, Tatsuro
	NRID 1000080599241 1000080599241 ORCID 0000-0003-3913-7330 0000-0003-3913-7330 researchmap permalink Jun-chi_Kishikawa Jun-chi_Kishikawa Scopus Author ID 35322447700 35322447700 CreatorName Kishikawa, Junichi
	ORCID 0000-0001-8991-587X 0000-0001-8991-587X researchmap permalink mhiro_map mhiro_map Scopus Author ID 55672764900 55672764900 CreatorName Hirose, Mika
	NRID 1000030790985 1000030790985 researchmap permalink miki_kinoshita miki_kinoshita Scopus Author ID 35310858600 35310858600 CreatorName Kinoshita, Miki
	NRID 1000070420362 1000070420362 CreatorName Kojima, Seiji
	NRID 1000020402993 1000020402993 researchmap permalink tohru_minamino tohru_minamino Scopus Author ID 7006391123 7006391123 CreatorName Minamino, Tohru
	NRID 1000030326300 1000030326300 CreatorName Uchihashi, Takayuki
	NRID 1000020423155 1000020423155 ORCID 0000-0002-8879-6685 0000-0002-8879-6685 researchmap permalink tkato_ipr tkato_ipr Scopus Author ID 55261010900 55261010900 CreatorName Kato, Takayuki
	NRID 1000040346143 1000040346143 ORCID 0000-0003-1342-8885 0000-0003-1342-8885 researchmap permalink read0096832 read0096832 Scopus Author ID 7006628770 7006628770 CreatorName Imada, Katsumi
	NRID 1000050209342 1000050209342 CreatorName Homma, Michio
Subject	flagellar motor
	MS-ring
	C-ring
	basal body
Description	Takekawa Norihiro, Nishikino Tatsuro, Kishikawa Jun-ichi, et al. Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor. mBio, e01261-24 (2024); https://doi.org/10.1128/mbio.01261-24.
Abstract	The marine bacterium Vibrio alginolyticus possesses a polar flagellum driven by a sodium ion flow. The main components of the flagellar motor are the stator and rotor. The C-ring and MS-ring, which are composed of FliG and FliF, respectively, are parts of the rotor. Here, we purified an MS-ring composed of FliF–FliG fusion proteins and solved the near-atomic resolution structure of the S-ring—the upper part of the MS-ring—using cryo-electron microscopy. This is the first report of an S-ring structure from Vibrio, whereas, previously, only those from Salmonella have been reported. The Vibrio S-ring structure reveals novel features compared with that of Salmonella, such as tilt angle differences of the RBM3 domain and the β-collar region, which contribute to the vertical arrangement of the upper part of the β-collar region despite the diversity in the RBM3 domain angles. Additionally, there is a decrease of the inter-subunit interaction between RBM3 domains, which influences the efficiency of the MS-ring formation in different bacterial species. Furthermore, although the inner-surface electrostatic properties of Vibrio and Salmonella S-rings are altered, the residues potentially interacting with other flagellar components, such as FliE and FlgB, are well structurally conserved in the Vibrio S-ring. These comparisons clarified the conserved and non-conserved structural features of the MS-ring across different species.
Publisher	American Society for Microbiology
Source Title	mBio
Volume (Issue)	15(10)
Page	e01261-24
Date of Issued	2024-09-06
Language	English
Handle URL	https://hdl.handle.net/11094/98250
eISSN	21507511
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1128/mbio.01261-24
Access Rights	open access
CopyRight	This article is licensed under a Creative Commons Attribution 4.0 International License.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCTERMS.bibliographicCitation	mBio. 2024, 15(10), p. e01261-24
DC.title	Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor
DC.creator	Takekawa, Norihiro
	Nishikino, Tatsuro
	Kishikawa, Junichi
	Hirose, Mika
	Kinoshita, Miki
	Kojima, Seiji
	Minamino, Tohru
	Uchihashi, Takayuki
	Kato, Takayuki
	Imada, Katsumi
	Homma, Michio
DC.publisher	American Society for Microbiology
DC.language' scheme='DCTERMS.RFC1766	English
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2024-09-06
DC.identifier	https://doi.org/10.1128/mbio.01261-24
DC.subject	flagellar motor
	MS-ring
	C-ring
	basal body
DC.description	Takekawa Norihiro, Nishikino Tatsuro, Kishikawa Jun-ichi, et al. Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor. mBio, e01261-24 (2024); https://doi.org/10.1128/mbio.01261-24.
DCTERMS.abstract	The marine bacterium Vibrio alginolyticus possesses a polar flagellum driven by a sodium ion flow. The main components of the flagellar motor are the stator and rotor. The C-ring and MS-ring, which are composed of FliG and FliF, respectively, are parts of the rotor. Here, we purified an MS-ring composed of FliF–FliG fusion proteins and solved the near-atomic resolution structure of the S-ring—the upper part of the MS-ring—using cryo-electron microscopy. This is the first report of an S-ring structure from Vibrio, whereas, previously, only those from Salmonella have been reported. The Vibrio S-ring structure reveals novel features compared with that of Salmonella, such as tilt angle differences of the RBM3 domain and the β-collar region, which contribute to the vertical arrangement of the upper part of the β-collar region despite the diversity in the RBM3 domain angles. Additionally, there is a decrease of the inter-subunit interaction between RBM3 domains, which influences the efficiency of the MS-ring formation in different bacterial species. Furthermore, although the inner-surface electrostatic properties of Vibrio and Salmonella S-rings are altered, the residues potentially interacting with other flagellar components, such as FliE and FlgB, are well structurally conserved in the Vibrio S-ring. These comparisons clarified the conserved and non-conserved structural features of the MS-ring across different species.
DC.rights	This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	98250
citation_title	Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor
citation_author	Takekawa, Norihiro
	Nishikino, Tatsuro
	Kishikawa, Junichi
	Hirose, Mika
	Kinoshita, Miki
	Kojima, Seiji
	Minamino, Tohru
	Uchihashi, Takayuki
	Kato, Takayuki
	Imada, Katsumi
	Homma, Michio
citation_publisher	American Society for Microbiology
citation_language	English
citation_date	2024-09-06
citation_journal_title	mBio
citation_volume	15
citation_issue	10
citation_firstpage	e01261-24
citation_doi	https://doi.org/10.1128/mbio.01261-24
citation_public_url	https://hdl.handle.net/11094/98250

Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor

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