The coupling region of F0F1 ATP synthase: binding of the hydrophilic loop of F0 subunit c to F1

FEBS Letters

Licher, T¹  Kellner, E¹  Lill, H¹ 

[1] Abteilung Biophysik, Universität Osnabrück, D-49069 Osnabrück, Germany

关键词: ATP synthase;    ATPase;    F0F1;    Proteolipid;    Coupling;    CF1;    spinach chloroplast F1 ATPase;    CF1(−δϵ);    CF1 lacking subunits δ and ϵ;    Coumarin;    7-diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarin;    Fluorescein;    fluorescein-5-maleimide;    FRET;    fluorescence resonance energy transfer;    PCR;    polymerase chain reaction;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    Tris;    N-tris-(hydroxymethyl)-aminomethane;   

DOI  :  10.1016/S0014-5793(98)00807-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The hydrophilic loop region of the CF₀ c subunit has been expressed as a fusion with MalE in Escherichia coli. A cysteine was introduced at the C-terminus to allow fluorophore labeling of the fusion protein. After removal of the MalE moiety, the labeled peptide was used for binding studies with fluorophore-labeled CF₁. At saturation, 1 mol peptide was bound per mol CF₁. Binding was abolished after removal of subunit ϵ from CF₁, and partially restored by addition of recombinant ϵ.

【 授权许可】

Unknown