Chemotactic responses to an attractant and a repellent by the polar and lateral flagellar systems of Vibrio alginolyticus

Article Abstract:

Vibrio alginolyticus has two types of flagellar systems, polar flagella and lateral flagella. Upon treatment with phenol, lateral-flagella-defective (Pof+ Laf-) mutants exhibited a tumbling state which is characterized by frequent forward and backward movements. A tethered-cell method revealed that this motion was due to the frequent changing of direction of motion of the flagellar motor. Treatment of cells with attractant serine abolished the tumbling motion and cells swam smoothly. In contrast, phenol treatment had no effect on polar-flagella-defective mutants, suggesting that lateral flagella can adapt to repellent stimulus.

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Characterization of polar-flagellar-length mutants in Vibrio alginolyticus

Article Abstract:

Swarm-deficient Vibrio alginolyticus mutants were isolated from a Laf-defective mutant were analyzed to characterize the mechanisms that modulates flagellar length during the flagellar protein assembly. Analysis of Pof-defective strains indicated the presence of three groups of mutants that were designated as chemotaxis-defective, flagellation-defective and motility-defective strains. The wild-type and mutant strains also exhibited swimming speeds that were dependent on sodium concentration.

Physiological aspects, Morphogenesis, Microbial mutation

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Random mutagenesis of the pomA gene encoding a putative channel component of the Na+-driven polar flagellar motor of Vibrio alginolyticus

Article Abstract:

Random mutagenesis of the pomA gene encoding a putative channel component of the Na+-driven polar flagellar motor of Vibrio alginolyticus was conducted to identify residues responsible for the function of PomA. Thirty-seven non-motile mutants were isolated and 26 independent mutations in the pomA gene were identified. Results demonstrate that the mutant proteins that exhibit dominance are expressed and inserted into the motor but do not function properly.

Membrane proteins, Mutagenesis

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