Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries

Kinoshita, Miki; Makino, Fumiaki; Miyata, Tomoko; Imada, Katsumi; Namba, Keiichi; Minamino, Tohru

doi:https://doi.org/10.1038/s42003-025-07485-2

Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries

Kinoshita, Miki; Makino, Fumiaki; Miyata, Tomoko et al.

Communications Biology, 2025, 8(1), 61

Number of Access:784（2025-08-15 06:45 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/101051

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Title	Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries
Creator	NRID 1000030790985 1000030790985 researchmap permalink miki_kinoshita miki_kinoshita Scopus Author ID 35310858600 35310858600 CreatorName Kinoshita, Miki
	CreatorName Makino, Fumiaki
	NRID 1000030423156 1000030423156 researchmap permalink miya_t miya_t Scopus Author ID 7401764889 7401764889 CreatorName Miyata, Tomoko
	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 1000030346142 1000030346142 researchmap permalink read0096830 read0096830 CreatorName Namba, Keiichi
	NRID 1000020402993 1000020402993 researchmap permalink tohru_minamino tohru_minamino Scopus Author ID 7006391123 7006391123 CreatorName Minamino, Tohru
Description	Kinoshita M., Makino F., Miyata T., et al. Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries. Communications Biology 8, 61 (2025); https://doi.org/10.1038/s42003-025-07485-2.
Abstract	The flagellar MS-ring is the initial template for flagellar assembly and houses the flagellar protein export complex. The MS-ring has three parts of different symmetries within the ring structure by assembly of FliF subunits in two different conformations with distinct arrangements of three ring-building motifs, RBM1, RBM2, and RBM3. However, it remains unknown how these symmetries are generated. A combination of cryoEM structure and structure-based mutational analyses demonstrates that the well-conserved DQxGxxL motif in the RBM2-RBM3 hinge loop allows RBM2 to take two different orientations relative to RBM3. Of 34 FliF subunits of the MS-ring in the basal body, 23 RBM2 domains form an inner ring with a central pore that accommodates the flagellar protein export complex, and the remaining 11 RBM2 domains form 11 cog-like structures together with RBM1 domains just outside the inner RBM2-ring. We propose that a dimer of FliF with two different conformations initiates MS-ring assembly.
Publisher	Nature Research
Source Title	Communications Biology
Volume (Issue)	8(1)
Page	61
Date of Issued	2025-01-16
Language	English
Handle URL	https://hdl.handle.net/11094/101051
eISSN	23993642
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1038/s42003-025-07485-2
Access Rights	open access
CopyRight	This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 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	Communications Biology. 2025, 8(1), p. 61
DC.title	Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries
DC.creator	Kinoshita, Miki
	Makino, Fumiaki
	Miyata, Tomoko
	Imada, Katsumi
	Namba, Keiichi
	Minamino, Tohru
DC.publisher	Nature Research
DC.language' scheme='DCTERMS.RFC1766	English
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2025-01-16
DC.identifier	https://doi.org/10.1038/s42003-025-07485-2
DC.description	Kinoshita M., Makino F., Miyata T., et al. Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries. Communications Biology 8, 61 (2025); https://doi.org/10.1038/s42003-025-07485-2.
DCTERMS.abstract	The flagellar MS-ring is the initial template for flagellar assembly and houses the flagellar protein export complex. The MS-ring has three parts of different symmetries within the ring structure by assembly of FliF subunits in two different conformations with distinct arrangements of three ring-building motifs, RBM1, RBM2, and RBM3. However, it remains unknown how these symmetries are generated. A combination of cryoEM structure and structure-based mutational analyses demonstrates that the well-conserved DQxGxxL motif in the RBM2-RBM3 hinge loop allows RBM2 to take two different orientations relative to RBM3. Of 34 FliF subunits of the MS-ring in the basal body, 23 RBM2 domains form an inner ring with a central pore that accommodates the flagellar protein export complex, and the remaining 11 RBM2 domains form 11 cog-like structures together with RBM1 domains just outside the inner RBM2-ring. We propose that a dimer of FliF with two different conformations initiates MS-ring assembly.
DC.rights	This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
DC.format	101051
citation_title	Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries
citation_author	Kinoshita, Miki
	Makino, Fumiaki
	Miyata, Tomoko
	Imada, Katsumi
	Namba, Keiichi
	Minamino, Tohru
citation_publisher	Nature Research
citation_language	English
citation_date	2025-01-16
citation_journal_title	Communications Biology
citation_volume	8
citation_issue	1
citation_firstpage	61
citation_doi	https://doi.org/10.1038/s42003-025-07485-2
citation_public_url	https://hdl.handle.net/11094/101051

Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries

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