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Lack of ability of trypsin‐treated mitochondrial F 1 ‐ATPase to bind the oligomycin‐sensitivity conferring protein (OSCP)
Author(s) -
Hundal Torill,
Norling Birgitta,
Ernster Lars
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81038-2
Subject(s) - oligomycin , trypsin , atpase , chemistry , biochemistry , biophysics , biology , enzyme
Soluble beef‐heart mitochondrial F 1 ‐ATPase modified in its α‐subunit by mild trypsin treatment (α′‐F 1 ) can no longer bind oligomycin‐sensitivity conferring protein (OSCP) but is still capable of binding to F 1 ‐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′‐F 1 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 (F 1 ) 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.