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Vacuolar ATPases (V-ATPases) function as proton pumps in various cellular membrane systems. The hydrophilic V 1  portion of the V-ATPase is a rotary motor, in which a central-axis DF complex rotates inside a hexagonally arranged catalytic A 3 B 3  complex by using ATP hydrolysis energy. We have previously reported crystal structures ofEnterococcushiraeV-ATPase A 3 B 3  and A 3 B 3 DF (V 1 ) complexes; the result suggested that the DF axis induces structural changes in the A 3 B 3  complex through extensive protein-protein interactions. In this study, we mutated 10 residues at the interface between A 3 B 3  and DF complexes and examined the ATPase activities of the mutated V 1  complexes as well as the binding affinities between the mutated A 3 B 3  and DF complexes. Surprisingly, several V 1  mutants showed higher initial ATPase activities than wild-type V 1 -ATPase, whereas these mutated A 3 B 3  and DF complexes showed decreased binding affinities for each other. However, the high ATP hydrolysis activities of the mutants decreased faster over time than the activity of the wild-type V 1  complex, suggesting that the mutants were unstable in the reaction because the mutant A 3 B 3  and DF complexes bound each other more weakly. These findings suggest that strong interaction between the DF complex and A 3 B 3  complex lowers ATPase activity, but also that the tight binding is responsible for the stable ATPase activity of the complex.

Loose Binding of the DF Axis with the A3B3 Complex Stimulates the Initial Activity of Enterococcus hirae V1-ATPase