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The coupling region of F 0 F 1 ATP synthase: binding of the hydrophilic loop of F 0 subunit c to F 1
Author(s) -
Licher T,
Kellner E,
Lill H
Publication year - 1998
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/s0014-5793(98)00807-2
Subject(s) - protein subunit , fusion protein , atp synthase , peptide , fluorophore , moiety , cysteine , recombinant dna , escherichia coli , chemistry , n terminus , stereochemistry , biochemistry , enzyme , fluorescence , peptide sequence , physics , quantum mechanics , gene
The hydrophilic loop region of the CF 0 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 CF 1 . At saturation, 1 mol peptide was bound per mol CF 1 . Binding was abolished after removal of subunit ϵ from CF 1 , and partially restored by addition of recombinant ϵ.