The prokaryotic thermophilic TF1‐ATPase is functionally compatible with the eukaryotic CFo‐part of the chloroplast ATP‐synthase

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Abstract
The ATP synthase from chloroplasts, CFo · F1, was reconstituted into liposomes, from which most of CF1 was removed by a short treatment with guanidinium chloride. ATP-dependent proton uptake was restored with these CFo-liposomes even better by the addition of the bacterial TF1- than of the related CF1-part. This proton uptake was prevented by tentoxin, a specific inhibitor of the CF1-ATPase, in these CFo · F1-liposomes, but not in the hybrid CFo · TF1-liposomes. Venturicidin, a specific inhibitor of proton flow through CFo, was able to block it in both the hybrid CFo· TF1-liposomes and reconstituted CFo· F1-liposomes. These results indicate that the bacterial TF1-part binds to the eukaryotic CFo-part of four subunits forming a functional CFo · TF1-ATPase.

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