Johnathan Turner, 2010, Molecular Biology
Studies of bacterial protein localization give insight into the fundamentals of intracellular structure and provide opportunities for developing novel antimicrobial therapeutics. Studies of polar flagellar localization in the opportunistic pathogen Pseudomonas aeruginosa have shown that a polar-localized protein, FlhF, is responsible for localizing the flagellum to the pole. Motility screens of a P. aeruginosa transposon mutant library isolated three proteins necessary for polar localization of FlhF and, thus, the flagellum.
These proteins, PA0406, PA2982, and PA2983, are homologous to the components of the conserved TonB energy transduction complex, suggest- ing a flagellar localization complex with functional homology to the TonB complex. Current work is focused on demonstrating complex formation by co-precipitation of the component proteins, and on establishing a system for direct observation of the dynamics of related proteins, including FlhF, during the process of Pseudomonas pathogenesis in the amoeba Dictyostelium discoideum and human tissue culture.