The prokaryotic thermophilic TF1-ATPase is functionally compatible with the eukaryotic CFo-part of the chloroplast ATP-synthase.
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.
Galmiche
J M
JM
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Pezennec
S
S
Zhao
R
R
Girault
G
G
Baeuerlein
E
E
D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D001419:Bacteria / Q000201:enzymology*; D002736:Chloroplasts / Q000201:enzymology*; D008081:Liposomes / Q000378:metabolism; D010456:Peptides, Cyclic / Q000494:pharmacology; D055503:Protein Multimerization; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011522:Protons; D014698:Venturicidins / Q000494:pharmacology
D008081:Liposomes; D010456:Peptides, Cyclic; D011522:Protons; D014698:Venturicidins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; C003384:tentoxin