Polar confinement of a macromolecular machine by an SRP-type GTPase

Anita Dornes, Lisa Marie Schmidt, Christopher-Nils Mais, John C. Hook, Jan Pané-Farré, Dieter Kressler, Kai Thormann () and Gert Bange ()
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Anita Dornes: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry
Lisa Marie Schmidt: Department of Microbiology and Molecular Biology
Christopher-Nils Mais: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry
John C. Hook: Department of Microbiology and Molecular Biology
Jan Pané-Farré: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry
Dieter Kressler: Department of Biology
Kai Thormann: Department of Microbiology and Molecular Biology
Gert Bange: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry

Nature Communications, 2024, vol. 15, issue 1, 1-11

Abstract: Abstract The basal structure of the bacterial flagellum includes a membrane embedded MS-ring (formed by multiple copies of FliF) and a cytoplasmic C-ring (composed of proteins FliG, FliM and FliN). The SRP-type GTPase FlhF is required for directing the initial flagellar protein FliF to the cell pole, but the mechanisms are unclear. Here, we show that FlhF anchors developing flagellar structures to the polar landmark protein HubP/FimV, thereby restricting their formation to the cell pole. Specifically, the GTPase domain of FlhF interacts with HubP, while a structured domain at the N-terminus of FlhF binds to FliG. FlhF-bound FliG subsequently engages with the MS-ring protein FliF. Thus, the interaction of FlhF with HubP and FliG recruits a FliF-FliG complex to the cell pole. In addition, the modulation of FlhF activity by the MinD-type ATPase FlhG controls the interaction of FliG with FliM-FliN, thereby regulating the progression of flagellar assembly at the pole.

Date: 2024
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DOI: 10.1038/s41467-024-50274-4

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