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The biosynthesis of type IV pili in the periplasm of Gram negative bacteria involves a multi-protein apparatus which assembles on the inner membrane. It is composed of a helical base (TFP) composed of a sheath (TFP-sheath) and a filament emerging from the sheath (TFP-PilT-PilF). The assembly of this piston-like structure allows retraction from the surface. The retraction mechanism is currently unknown, yet is thought to be accomplished through the inward movement of the tip of the filament against a solid back wall. In this work, we used AFM to study the retraction force of the TFP and the associated surface translocation. We found that the retraction forces are strictly nonlinear. The derived retraction force reaches up to 23 pN at 20 nm retraction. The retraction force is small at short retraction (less than 8 nm only) and increases significantly at around 20 nm and saturates sharply. The saturation behavior of the retraction force suggests that the surface translocation becomes kinetically controlled when the retraction distance is less than 20 nm and reaches a plateau at around 20 nm. The dependence of the retraction force on the retraction distance suggests an elastic model for the retraction process. In the elastic model, the retraction force originates from the elasticity of the TFP and the retraction force is proportional to the elongation of the sheath.
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