The γ subunit of F1 and the PVP protein of Fo (FoI) are components of the gate of the mitochondrial FoF1 H+‐ATP synthase

FEBS Letters

Guerrieri, F.¹  Papa, S.¹  Fiermonte, M.¹  Jirillo, E.²  Capozza, G.¹  Zanotti, F.¹ 

[1] Institute of Medical Biochemistry and Chemistry, Centre for the Study of Mitochondria and Energy Metabolism, University of Bari, Bari, Italy;Institute of Immunology, University of Bari, Bari, Italy

关键词: H+-ATP synthase;    Diamide;    Thiol group;    F1;    Fo;    Chaps;    3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate;    SDS-PAGE;    sodium dodecylsulphate-polyacryl-amide gel electrophoresis;    USMP;    urea-treated submitochondrial particles;    DCCD;    N;    N'-dicyclohexylcarbodiimide;    NEM;    N-ethyl-maleimide;    PVP;    protein (FoI);    OSCP;    subunits of the membrane sector Fo;   

DOI  :  10.1016/0014-5793(90)80462-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The γ subunit of the F₁ moiety of the bovine mitochondrial H⁺-ATP synthase is shown to function as a component of the gate. Addition of purified γ subunit to F_o-liposomes inhibits transmembrane proton conduction. This inhibition can be removed by the bifunctional thiol reagent diamide. Immunoblot analysis shows that the diamide effect is likely due to disulphide bridging of the γ subunit with the PVP protein of the F_o sector.

【 授权许可】

Unknown