1. Polar confinement of a macromolecular machine by an SRP-type GTPase.
- Author
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Dornes A, Schmidt LM, Mais CN, Hook JC, Pané-Farré J, Kressler D, Thormann K, and Bange G
- Subjects
- Protein Binding, GTP Phosphohydrolases metabolism, GTP Phosphohydrolases chemistry, GTP Phosphohydrolases genetics, Signal Recognition Particle metabolism, Signal Recognition Particle chemistry, Monomeric GTP-Binding Proteins metabolism, Monomeric GTP-Binding Proteins chemistry, Monomeric GTP-Binding Proteins genetics, Membrane Proteins, Flagella metabolism, Bacterial Proteins metabolism, Bacterial Proteins chemistry, Bacterial Proteins genetics
- 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., (© 2024. The Author(s).)
- Published
- 2024
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