The prokaryotic thermophilic TF 1-ATPase is functionally compatible with the eukaryotic CF o-part of the chloroplast ATP-synthase

• Published in: FEBS letters Vol. 338; no. 2; pp. 152 - 156
• Main Authors: Galmiche, Jean Michel, Pezennec, Stephane, Zhao, Rongbao, Girault, Guy, Baeuerlein, Edmund
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 31.01.1994; Wiley
• Subjects: Biochemistry; Biochemistry, Molecular Biology; CF o · TF 1-ATP synthase; Functional compatibility; Life Sciences; Reconstruction (in vitro); Spinach chloroplast; Thermophilic bacterium PS3; Vegetal Biology; Thermophilic bacterium PS3; GCL, guanidinium chloride; [ 125I]ASA-ßala-OH, 3[ 125Iodo]-4-azido-2-hydroxybenzoyl-β-alanine; EDTA, ethylenediaminetetraacetic acid; CHAPS,3-[(cholamidopropyl)-dimethyl-ammonio]-1-propane sulfate; Reconstruction (in vitro); FCCP, carbonyl cyamide- p-trifuorohydroxyphenyl hydrazone; Spinach chloroplast; Functional compatibility; ACMA, 9-amino-6-chloro-2-methoxy-acridine; DCCD,dicyclohexylcarbodiimide; Tricine, N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl] glycine; CF o · TF 1-ATP synthase; DTT, d, l-dithio-threitol
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(94)80354-4

The ATP synthase from chloroplasts, CF o · F 1, was reconstituted into liposomes, from which most of CF 1 was removed by a short treatment with guanidinium chloride. ATP-dependent proton uptake was restored with these CF o-liposomes even better by the addition of the bacterial TF 1- than of the related CF 1-part. This proton uptake was prevented by tentoxin, a specific inhibitor of the CF 1-ATPase, in these CF o · F 1-liposomes, but not in the hybrid CF o · TF 1-liposomes. Venturicidin, a specific inhibitor of proton flow through CF o, was able to block it in both the hybrid CF o· TF 1-liposomes and reconstituted CF o· F 1-liposomes. These results indicate that the bacterial TF 1-part binds to the eukaryotic CF o-part of four subunits forming a functional CF o · TF 1-ATPase.