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

[摘要]

The ATP synthase from chloroplasts, CF_o · 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 CF_o-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 CF_o · F₁-liposomes, but not in the hybrid CF_o · TF₁-liposomes. Venturicidin, a specific inhibitor of proton flow through CF_o, was able to block it in both the hybrid CF_o· TF₁-liposomes and reconstituted CF_o· F₁-liposomes. These results indicate that the bacterial TF₁-part binds to the eukaryotic CF_o-part of four subunits forming a functional CF_o · TF₁-ATPase.

[学科分类] 生物化学/生物物理

[关键词] Thermophilic bacterium PS3;Spinach chloroplast;CFo · TF1-ATP synthase;Reconstruction (in vitro);Functional compatibility;ACMA;9-amino-6-chloro-2-methoxy-acridine;CHAPS;3-[(cholamidopropyl)-dimethyl-ammonio]-1-propane sulfate;DCCD;dicyclohexylcarbodiimide;DTT;d;l-dithio-threitol;EDTA;ethylenediaminetetraacetic acid;FCCP;carbonyl cyamide-p-trifuorohydroxyphenyl hydrazone;GCL;guanidinium chloride;[125I]ASA-ßala-OH;3[125Iodo]-4-azido-2-hydroxybenzoyl-β-alanine;Tricine;N-[2-hydroxy-1;1-bis(hydroxymethyl)ethyl] glycine