{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Arroyo-Perez EE"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["RP93004"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11620751"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["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 <i>Vibrio parahaemolyticus</i>, <i>Pseudomonas putida</i>, and <i>Shewanella putrefaciens</i>, and it does so independently of the polar localization mediated by HubP. FipA exhibits a dynamic localizati"],"journal":["eLife"],"pubmed_title":["A conserved cell-pole determinant organizes proper polar flagellum formation."],"pmcid":["PMC11620751"],"funding_grant_id":["TRR 174-P12"],"pubmed_authors":["Hook JC","Arroyo-Perez EE","Wimmi S","Glatter T","Ringgaard S","Alvarado A","Thormann K"],"additional_accession":[]},"is_claimable":false,"name":"A conserved cell-pole determinant organizes proper polar flagellum formation.","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 <i>Vibrio parahaemolyticus</i>, <i>Pseudomonas putida</i>, and <i>Shewanella putrefaciens</i>, and it does so independently of the polar localization mediated by HubP. FipA exhibits a dynamic localizati","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-06-02T10:48:44.777Z","creation":"2025-04-03T23:52:00.641Z"},"accession":"S-EPMC11620751","cross_references":{"pubmed":["39636223"],"doi":["10.7554/eLife.93004"]}}