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

FEBS Letters

Zhao, Rongbao²  Baeuerlein, Edmund²  Girault, Guy¹  Pezennec, Stephane¹  Galmiche, Jean Michel¹ 

[1] Centre d'Etudes de Saclay, Département de Biologie Cellulaire et Moléculaire, Section Bioénergétique, F-91191 Gif-sur-Yvette, France;Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany

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;   

DOI  :  10.1016/0014-5793(94)80354-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown