The coupling region of F0F1 ATP synthase: binding of the hydrophilic loop of F-0 subunit c to F-1

Autor(en): Licher, T
Kellner, E
Lill, H
Stichwörter: ATP synthase; ATPase; Biochemistry & Molecular Biology; Biophysics; Cell Biology; CHLOROPLAST; COMPLEX; coupling; EPSILON; ESCHERICHIA-COLI; F0F1; F1; F1-ATPASE; proteolipid
Erscheinungsdatum: 1998
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEBS LETTERS
Volumen: 431
Ausgabe: 3
Startseite: 419
Seitenende: 422
Zusammenfassung: 
The hydrophilic loop region of the CF0 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 CF1. At saturation, 1 mol peptide mas bound per mol CF1. Binding was abolished after removal of subunit epsilon from CF1, and partially restored by addition of recombinant epsilon. (C) 1998 Federation of European Biochemical Societies.
ISSN: 00145793
DOI: 10.1016/S0014-5793(98)00807-2

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