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F 1 - and V 1 -ATPase are rotary molecular motors that convert chemical energy released upon ATP hydrolysis into torque to rotate a central rotor axle against the surrounding catalytic stator cylinder with high efficiency. How conformational change occurring in the stator is coupled to the rotary motion of the axle is the key unknown in the mechanism of rotary motors. Here, we generated chimeric motor proteins by inserting an exogenous rod protein, FliJ, into the stator ring of F 1 or of V 1 and tested the rotation properties of these chimeric motors. Both motors showed unidirectional and continuous rotation, despite no obvious homology in amino acid sequence between FliJ and the intrinsic rotor subunit of F 1 or V 1 These results showed that any residue-specific interactions between the stator and rotor are not a prerequisite for unidirectional rotation of both F 1 and V 1 The torque of chimeric motors estimated from viscous friction of the rotation probe against medium revealed that whereas the F 1 -FliJ chimera generates only 10% of WT F 1 , the V 1 -FliJ chimera generates torque comparable to that of V 1 with the native axle protein that is structurally more similar to FliJ than the native rotor of F 1 This suggests that the gross structural mismatch hinders smooth rotation of FliJ accompanied with the stator ring of F 1 .

Rotation of artificial rotor axles in rotary molecular motors