A conserved cell-pole determinant organizes proper polar flagellum formation
The coordination of cell cycle progression and flagellar synthesis is a complex process in motile bacteria. In γ-proteobacteria, the localization of the flagellum to the cell pole is mediated by the SRP-type GTPase FlhF. However, the mechanism of action of FlhF, and its relationship with the cell po...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2024-12-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/93004 |
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| author | Erick E Arroyo-Pérez John C Hook Alejandra Alvarado Stephan Wimmi Timo Glatter Kai Thormann Simon Ringgaard |
| author_facet | Erick E Arroyo-Pérez John C Hook Alejandra Alvarado Stephan Wimmi Timo Glatter Kai Thormann Simon Ringgaard |
| author_sort | Erick E Arroyo-Pérez |
| collection | DOAJ |
| description | The coordination of cell cycle progression and flagellar synthesis is a complex process in motile bacteria. In γ-proteobacteria, the localization of the flagellum to the cell pole is mediated by the SRP-type GTPase FlhF. However, the mechanism of action of FlhF, and its relationship with the cell pole landmark protein HubP remain unclear. In this study, we discovered a novel protein called FipA that is required for normal FlhF activity and function in polar flagellar synthesis. We demonstrated that membrane-localized FipA interacts with FlhF and is required for normal flagellar synthesis in Vibrio parahaemolyticus, Pseudomonas putida, and Shewanella putrefaciens, and it does so independently of the polar localization mediated by HubP. FipA exhibits a dynamic localization pattern and is present at the designated pole before flagellar synthesis begins, suggesting its role in licensing flagellar formation. This discovery provides insight into a new pathway for regulating flagellum synthesis and coordinating cellular organization in bacteria that rely on polar flagellation and FlhF-dependent localization. |
| format | Article |
| id | doaj-art-0fb5495b15fc43f2afa2b09495416772 |
| institution | OA Journals |
| issn | 2050-084X |
| language | English |
| publishDate | 2024-12-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj-art-0fb5495b15fc43f2afa2b094954167722025-08-20T02:19:10ZengeLife Sciences Publications LtdeLife2050-084X2024-12-011310.7554/eLife.93004A conserved cell-pole determinant organizes proper polar flagellum formationErick E Arroyo-Pérez0John C Hook1Alejandra Alvarado2Stephan Wimmi3Timo Glatter4Kai Thormann5https://orcid.org/0000-0001-7292-4884Simon Ringgaard6Max Planck Institute for Terrestrial Microbiology, Department of Ecophysiology, Munich, Germany; Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, GermanyDepartment of Microbiology and Molecular Biology, Justus-Liebig-Universität Giessen, Giessen, GermanyInterfaculty Institute of Microbiology and Infection Medicine Tübingen, Bacterial Metabolomics, University of Tübingen, Tübingen, GermanyMax Planck Institute for Terrestrial Microbiology, Department of Ecophysiology, Munich, Germany; Institute for Biological Physics, University of Cologne, Köln, GermanyCore Facility for Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Marburg, GermanyDepartment of Microbiology and Molecular Biology, Justus-Liebig-Universität Giessen, Giessen, GermanyMax Planck Institute for Terrestrial Microbiology, Department of Ecophysiology, Munich, Germany; Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, GermanyThe coordination of cell cycle progression and flagellar synthesis is a complex process in motile bacteria. In γ-proteobacteria, the localization of the flagellum to the cell pole is mediated by the SRP-type GTPase FlhF. However, the mechanism of action of FlhF, and its relationship with the cell pole landmark protein HubP remain unclear. In this study, we discovered a novel protein called FipA that is required for normal FlhF activity and function in polar flagellar synthesis. We demonstrated that membrane-localized FipA interacts with FlhF and is required for normal flagellar synthesis in Vibrio parahaemolyticus, Pseudomonas putida, and Shewanella putrefaciens, and it does so independently of the polar localization mediated by HubP. FipA exhibits a dynamic localization pattern and is present at the designated pole before flagellar synthesis begins, suggesting its role in licensing flagellar formation. This discovery provides insight into a new pathway for regulating flagellum synthesis and coordinating cellular organization in bacteria that rely on polar flagellation and FlhF-dependent localization.https://elifesciences.org/articles/93004vibrio parahaemolyticusshewanella putrefaciensPseudomonas putida |
| spellingShingle | Erick E Arroyo-Pérez John C Hook Alejandra Alvarado Stephan Wimmi Timo Glatter Kai Thormann Simon Ringgaard A conserved cell-pole determinant organizes proper polar flagellum formation eLife vibrio parahaemolyticus shewanella putrefaciens Pseudomonas putida |
| title | A conserved cell-pole determinant organizes proper polar flagellum formation |
| title_full | A conserved cell-pole determinant organizes proper polar flagellum formation |
| title_fullStr | A conserved cell-pole determinant organizes proper polar flagellum formation |
| title_full_unstemmed | A conserved cell-pole determinant organizes proper polar flagellum formation |
| title_short | A conserved cell-pole determinant organizes proper polar flagellum formation |
| title_sort | conserved cell pole determinant organizes proper polar flagellum formation |
| topic | vibrio parahaemolyticus shewanella putrefaciens Pseudomonas putida |
| url | https://elifesciences.org/articles/93004 |
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