Structural and functional modifications induced by diamide on the F0 sector of the mammalian ATP synthase

FEBS Letters

Lippe, Giovanna²  Dabbeni-Sala, Federica¹  Sorgato, M.Catia² 

[1] Dipartimento de Farmacologia, Largo Meneghetti 7, 35131 Padova, Italy;Dipartimento di Chimica Biologica e Centro CNR per lo Studio della Fisiologia Mitrocondriale, Via Trieste 75, 35121 Padova, Italy

关键词: ATP synthase;    Mitochondria;    SH groups;    Diamide;    F0;    F1;    diamide;    diazenedicarboxylic acid bis(dimethylamide);    F1;    coupling factor 1 of ATP synthase;    F0;    hydrophobic part of ATP synthase;    OSCP;    oligomycin-sensitivity-conferring-protein;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    EDTA;    ethylenediaminetetraacetic acid;    AdNT;    adenine nucleotide translocator;    DCCD;    N;    N′-dicyclohexylcarbodiimide;   

DOI  :  10.1016/0014-5793(91)80355-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In this report data are presented which firmly establish that by treating isolated F₀ with the thiol reagent diamide, two 25 kDa F₀ subunits react to form a dimer of 45 kDa apparent molecular mass. This dimerising effect is correlated to the impairment of the binding of F₁ to F₀, both at μM and mM diamide concentrations. Under the latter condition, modification of other F₀ subunits also occurs. Passive proton conductance through F₀, as well as its sensitivity to N,N′-dicyclohexylcarbodiimide, are affected at low diamide concentration. Thus perturbation of the cysteine residue of the 25 kDd F₀ subunit is sufficient for altering the ATP synthase proton channel.

【 授权许可】

Unknown