Role of FlhF and its domains in the assembly of a polar flagellum in <i>P. aeruginosa</i>.

ABSTRACT: FlhF, an SRP GTPase, regulates the polarity and flagellation patterns in various bacteria, including Pseudomonas aeruginosa. FlhF is a multidomain protein that comprises three domains: B, N, and G, or the GTPase domain. However, the roles of different domains in the assembly and maintenance of flagella in this clinically important bacterium remain unclear. In this study, we report that the C-terminal GTPase domain plays a critical role in maintaining the polar localization of FlhF. Complementation assays using truncated constructs show that the flagellar assembly depends on both the B- and N-domains. In addition, GTP binding by FlhF regulates its interaction with FliG, a flagellar C-ring protein that facilitates flagellar basal body assembly in P. aeruginosa.IMPORTANCEPathoge

SUBMITTER: Raghav S 

PROVIDER: S-EPMC12713375 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature