Neighbouring subunits of CF0 and between CF1 and CF0 of the soluble chloroplast ATP synthase (CF1‐CF0) as revealed by chemical protein cross‐linking

FEBS Letters

Süss, Karl-Heinz¹ 

[1] Zentralinstitut für Genetik und Kulturpflanzenforschung, Akademie der Wissenschaften der DDR, 4325 Gatersleben, GDR

关键词: Chloroplast;    ATP synthase;    Cross-linking;    CF1-CF0interaction;    Neighboring subunits;    CF1 and CF0;    catalytic portion and membrane portion of the chloroplast ATP synthase;    respectively;    CuP;    copper phenanthroline;    DTBP;    dimethyl 3;    3́-dithiobispropionimidate;    DSP;    dithiobis(succinimidyl propionate);    2D-PAGE;    two-dimensional polyacrylamide gel electrophoresis;    MBI;    4-methylmercaptobutyrimidate;   

DOI  :  10.1016/0014-5793(86)80571-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Neighbouring subunits of CF₀ (I–III) and between cf₀ and CF₁ (α-ϵ) of the chloroplast ATP synthase have been examined by cross-linking with Cu-phenanthroline (CuP) and bifunctional, cleavable imidoesters. Imidoesters caused cross-links of α-II, β-I, β-II, γ-II, δ-I and ϵ-III as well as of I₂, I–III, II–III and III₂ of the CF₀ portion. subunits α-II, β-I, β-II, γ-II and I-I are close enough to form intermolecular cystine bridges upon CuP-catalyzed oxidation of sH groups. The results indicate that: (i) mainly interactions of the CF₁ subunits α, β and γ with the CF₀ polypeptides I and II are required for binding of CF₁ to the thylakoid membrane; (ii) subunit ϵ interacts directly with CF₀-III; (iii) the CF₀ portion contains a dimer of subunit I; (iv) subunits α and β appear to be structurally non-equivalent within the protein complex.

【 授权许可】

Unknown