Reconstitution of ATPase from the isolated subunits of coupling factor F1's of Escherichia coli and thermophilic bacterium PS3

ATPase was reconstituted from mixtures of isolated subunits of coupling factor, F₁ ATPase of E. coli (EF₁) and thermophilic bacterium PS3 (TF₁); ability to hydrolyze ATP was attained from the combination of α and β subunits from EF₁ and γ subunit from TF₁, α and β from TF₁ and γ from EF₁, and α and γ from EF₁ and β from TF₁. The β subunit of TF₁ also could complement the EF₁ from an E. coli mutant defective in this subunit. This is the first demonstration of interspecies in vitro recombination of ATPase activity from isolated subunits.