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

アクセス数:768件（2025-07-29 07:28 集計）

固定URL: https://hdl.handle.net/11094/101051

閲覧可能ファイル

ファイル	フォーマット	利用条件	サイズ	閲覧回数	利用開始日	説明	information
CommunBiolog_8_1	pdf	なし	5.85 MB	18	2025.04.18

Creative Commons : 表示 - 非営利 - 改変禁止

論文情報

ファイル出力 EndNote Basic出力 Mendeley出力

タイトル	Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries
著者	NRID 1000030790985 1000030790985 researchmap permalink miki_kinoshita miki_kinoshita Scopus Author ID 35310858600 35310858600 著者名 Kinoshita, Miki
	著者名 Makino, Fumiaki
	NRID 1000030423156 1000030423156 researchmap permalink miya_t miya_t Scopus Author ID 7401764889 7401764889 著者名 Miyata, Tomoko
	NRID 1000040346143 1000040346143 ORCID 0000-0003-1342-8885 0000-0003-1342-8885 researchmap permalink read0096832 read0096832 Scopus Author ID 7006628770 7006628770 著者名 Imada, Katsumi
	NRID 1000030346142 1000030346142 researchmap permalink read0096830 read0096830 著者名 Namba, Keiichi
	NRID 1000020402993 1000020402993 researchmap permalink tohru_minamino tohru_minamino Scopus Author ID 7006391123 7006391123 著者名 Minamino, Tohru
内容	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.
抄録	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.
出版者	Nature Research
収録物名	Communications Biology
巻(号)	8(1)
ページ	61
刊行年月	2025-01-16
言語	英語
ハンドルURL	https://hdl.handle.net/11094/101051
eISSN	23993642
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1038/s42003-025-07485-2
アクセス権	open access
権利情報	This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
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	英語
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	英語
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

閲覧可能ファイル

論文情報

論文詳細を表示