Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries
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...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-01-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-025-07485-2 |
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| author | Miki Kinoshita Fumiaki Makino Tomoko Miyata Katsumi Imada Keiichi Namba Tohru Minamino |
| author_facet | Miki Kinoshita Fumiaki Makino Tomoko Miyata Katsumi Imada Keiichi Namba Tohru Minamino |
| author_sort | Miki Kinoshita |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-d148576f3ce543828e328995ea9f535f |
| institution | Kabale University |
| issn | 2399-3642 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj-art-d148576f3ce543828e328995ea9f535f2025-01-19T12:35:39ZengNature PortfolioCommunications Biology2399-36422025-01-018111310.1038/s42003-025-07485-2Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetriesMiki Kinoshita0Fumiaki Makino1Tomoko Miyata2Katsumi Imada3Keiichi Namba4Tohru Minamino5Graduate School of Frontier Biosciences, Osaka UniversityGraduate School of Frontier Biosciences, Osaka UniversityGraduate School of Frontier Biosciences, Osaka UniversityDepartment of Macromolecular Science, Graduate School of Science, Osaka UniversityGraduate School of Frontier Biosciences, Osaka UniversityGraduate School of Frontier Biosciences, Osaka UniversityAbstract 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.https://doi.org/10.1038/s42003-025-07485-2 |
| spellingShingle | Miki Kinoshita Fumiaki Makino Tomoko Miyata Katsumi Imada Keiichi Namba Tohru Minamino Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries Communications Biology |
| title | Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries |
| title_full | Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries |
| title_fullStr | Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries |
| title_full_unstemmed | Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries |
| title_short | Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries |
| title_sort | structural basis for assembly and function of the salmonella flagellar ms ring with three different symmetries |
| url | https://doi.org/10.1038/s42003-025-07485-2 |
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