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