Lack of ability of trypsin‐treated mitochondrial F1‐ATPase to bind the oligomycin‐sensitivity conferring protein (OSCP)

FEBS Letters

Hundal, Torill¹  Ernster, Lars¹  Norling, Birgitta¹ 

[1] Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden

关键词: Oligomycin-sensitive ATPase;    F1-ATPase;    F1-subunit;    Oligomycin-sensitivity conferring protein;    Reconstitution;    Trypsin digestion;    Fo and F1;    proton-translocating and catalytic moieties of the mitochondrial ATPase system;    OSCP;    oligomycin-sensitivity conferring protein;    F6;    coupling factor 6;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(83)81038-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Soluble beef-heart mitochondrial F₁-ATPase modified in its α-subunit by mild trypsin treatment (α′-F₁) can no longer bind oligomycin-sensitivity conferring protein (OSCP) but is still capable of binding to F₁-depleted submitochondrial particles, giving rise to a maximally oligomycin-sensitive ATPase, provided the particles contain their native complement of OSCP. When OSCP is removed from the particles, α′-F₁ can still bind to the particles, but added OSCP induces only a low degree of oligomycin sensitivity. The possible role of OSCP in the functional coupling of the catalytic (F₁) and H⁺-translocating (F_o) moieties of mitochondrial ATPase is discussed. The results suggest a functional similarity between the OSCP component of mitochondrial ATPase and the δ-subunit of E. coli ATPase, which is in accordance with the structural homology recently found to exist between the two polypeptides.

【 授权许可】

Unknown