Abstract
The role of rotational molecular motors of the ATP synthase class is integral to the metabolism of cells. Yet the function of FliI(6)-FliJ complex, a homolog of the F(1) ATPase motor, within the flagellar export apparatus remains unclear. We use a simple two-state model adapted from studies of linear molecular motors to identify key features of this motor. The two states are the 'locked' ground state where the FliJ coiled coil filament experiences angular fluctuations in an asymmetric torsional potential, and a 'free' excited state in which FliJ undergoes rotational diffusion. Michaelis-Menten kinetics was used to treat transitions between these two states, and obtain the average angular velocity of the unloaded FliJ filament within the FliI(6) stator: ω(max) ≈ 9.0 rps. The motor was then studied under external counter torque conditions in order to ascertain its maximal power output: P(max) ≈ 42 k(B)T/s (or 102 kW/mol), and the stall torque: G(stall) ≈ 3 k(B)T/rad (or 0.01 nN·nm/rad). Two modes of action within the flagellar export apparatus are proposed, in which the motor performs useful work either by continuously 'grinding' through the resistive environment of the export gate, or by exerting equal and opposite stall force on it. In both cases, the resistance is provided by flagellin subunits entering the flagellar export channel prior to their unfolding. We therefore propose that the function of the FliI(6)-FliJ complex is to lower the energy barrier, and therefore assist in unfolding of the flagellar proteins before feeding them into the transport channel.