A flagellar accessory protein links chemotaxis to surface sensing.

Bacteria find suitable locations for colonization by sensing and responding to surfaces. Complex signaling repertoires control surface colonization, and surface contact sensing by the flagellum plays a central role in activating colonization programs. adheres to surfaces using a polysaccharide adhesin called the holdfast. In , disruption of the flagellum through interactions with a surface or mutation of flagellar genes increases holdfast production. Our group previously identified several genes involved in flagellar surface sensing. One of these, , codes for a protein with homology to the flagellar C-ring protein FliN. We show here that a fluorescently tagged FssF protein localizes to the flagellated pole of the cell and requires all components of the flagellar C-ring for proper localization, supporting the model that FssF associates with the C-ring. Deleting results in a severe motility defect, which we show is due to a disruption of chemotaxis. Epistasis experiments demonstrate that promotes adhesion through a stator-dependent pathway when late-stage flagellar mutants are disrupted. Separately, we find that disruption of chemotaxis through deletion of or other chemotaxis genes results in a hyperadhesion phenotype. Key genes in the surface sensing network (, , and ) contribute to both ∆dependent and ∆dependent hyperadhesion, but these genes affect adhesion differently in the two hyperadhesive backgrounds. Our results support a model in which the stator subunits of the flagella incorporate both mechanical and chemical signals to regulate adhesion.IMPORTANCEBacterial biofilms pose a threat in clinical and industrial settings. Surface sensing is one of the first steps in biofilm formation. Studying surface sensing can improve our understanding of biofilm formation and develop preventative strategies. In this study, we use the freshwater bacterium to study surface sensing and the regulation of surface attachment. We characterize a previously unstudied gene, , and find that it localizes to the cell pole in the presence of three proteins that make up a component of the flagellum called the C-ring. Additionally, we find that is required for chemotaxis behavior but dispensable for swimming motility. Lastly, our results indicate that deletion of and other genes required for chemotaxis results in a hyperadhesive phenotype. These results support that surface sensing requires chemotaxis for a robust response to a surface.