THE PROKARYOTIC THERMOPHILIC TF1-ATPASE IS FUNCTIONALLY COMPATIBLE WITH THE EUKARYOTIC CFO-PART OF THE CHLOROPLAST ATP-SYNTHASE

The ATP synthase from chloroplasts, CF0.F-1, was reconstituted into li posomes, from which most of CF1 was removed by a short treatment with guanidinium chloride. ATP-dependent proton uptake was restored with th ese CF0-liposomes even better by the addition of the bacterial TF1- th an of the related CF1-part. This proton uptake was prevented by tentox in, a specific inhibitor of the CF1-ATPase, in these CF0.F-1-liposomes , but not in the hybrid CF0.TF1-liposomes. Venturicidin, a specific in hibitor of proton flow through CF0, was able to block it in both the h ybrid CF0.TF1-liposomes and reconstituted CF0.F-1-liposomes. These res ults indicate that the bacterial TF1-part binds to the eukaryotic CF0- part of four subunits forming a functional CF0.TF1-ATPase.