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Vacuolar type rotary H + -ATPases (V o V 1 ) couple ATP synthesis/hydrolysis by V 1  with proton translocation by V o  via rotation of a central rotor apparatus composed of the V 1 -DF rotor shaft, a socket-like V o -C (eukaryotic V o -d) and the hydrophobic rotor ring. Reconstitution experiments using subcomplexes revealed a weak binding affinity of V 1 -DF to V o -C despite the fact that torque needs to be transmitted between V 1 -DF and V o -C for the tight energy coupling between V 1  and V o . Mutation of a short helix at the tip of V 1 -DF caused intramolecular uncoupling of V o V 1 , suggesting that proper fitting of the short helix of V 1 -D into the socket of V o -C is required for tight energy coupling between V 1  and V o . To account for the apparently contradictory properties of the interaction between V 1 -DF and V o -C (weak binding affinity but strict requirement for torque transmission), we propose a model in which the relationship between V 1 -DF and V o -C corresponds to that between a slotted screwdriver and a head of slotted screw. This model is consistent with our previous result in which the central rotor apparatus is not the major factor for the association of V 1  with V o  (Kishikawa and Yokoyama, J Biol Chem. 2012 24597-24603).

The Ingenious Structure of Central Rotor Apparatus in VoV1; Key for Both Complex Disassembly and Energy Coupling between V1 and Vo