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The mitochondrial ATP synthase inhibitor protein binds near the C‐terminus of the F 1 β‐subunit
Author(s) -
Jackson Philip J.,
Harris David A.
Publication year - 1988
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(88)80832-9
Subject(s) - atp synthase , atp synthase gamma subunit , protein subunit , atpase , biochemistry , mitochondrion , n terminus , inhibitor protein , enzyme , microbiology and biotechnology , biology , peptide sequence , chemistry , atp hydrolysis , gene
The specific, mitochondrial ATP synthase protein (IF 1 ) was covalently cross‐linked to its binding site on the catalytic sector of the enzyme (F 1 ‐ATPase). The cross‐linked complex was selectively cleaved, leaving IF 1 intact to facilitate the subsequent purification of the F 1 fragment to which IF 1 was cross‐linked. This fragment was identified by sequence analysis as comprising residues 394–459 on the F 1 β‐subunit, near the C‐terminus. This finding is discussed in the light of secondary structure predictions for both IF 1 and the F 1 β‐subunit, and sequence homologies between mitochondrial and other ATP synthases.