Summary: Purified adenosine triphosphatase (F-ATPase) (EC from membranes required divalent metal ions for its reattachment to membranes depleted of the enzyme. This requirement showed specificity: Mg ions were able to reconstitute a physiologically significant F-ATPase-membrane complex, whereas Zn ions produced one differing from the native and the Mg-reconstituted ATPase-membrane complexes. membranes contained a limited number of specific binding sites, which did not seem to be modified after ATPase release and membrane manipulation. The binding properties of F-ATPase preparations correlated well with their content of δ-subunit. The results suggested that F-ATPase molecules able to rebind to membranes must contain at least two copies of the δ-subunit. The isolated subunits (particularly α- and β-subunits) showed a certain capacity for rebinding to the membranes, but an enzyme form consisting only of α- and β-subunits was unable to reattach to membranes. These results prove unambiguously that δ-, but not α-or any other polypeptide, was involved in the attachment of F-ATPase to membranes, unlike other bacterial F-ATPases. These results were consistent with a subunit stoichiometry and arrangement: α β γ δ-Mg- membrane.


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