Fluorescence resonance energy transfer mapping of subunit delta in spinach chloroplast F-1 ATPase

Autor(en): Engelbrecht, S
Giakas, E
Marx, O
Lill, H
Stichwörter: ADENOSINE-TRIPHOSPHATASE; adenosinetriphosphatase; BINDING; Biochemistry & Molecular Biology; COUPLING FACTOR-I; CROSS-LINKING; ESCHERICHIA-COLI F1-ATPASE; F0F1 ATP synthase; fluorescence resonance energy transfer; PHOTOPHOSPHORYLATION; RECONSTITUTION; SELECTIVE MODIFICATION; SENSITIVITY CONFERRING PROTEIN; SYNTHASE
Erscheinungsdatum: 1998
Herausgeber: SPRINGER VERLAG
Journal: EUROPEAN JOURNAL OF BIOCHEMISTRY
Volumen: 252
Ausgabe: 2
Startseite: 277
Seitenende: 283
Zusammenfassung: 
Despite the considerable progress in the field of F0F1-ATPases caused by solving the 2.8-Angstrom structure of mitochondrial F-1 ATPase [Abrahams, J. P., Leslie, A. G. W., Lutter, R. & Walker, J. E. (1994) Nature 370, 621-628], little is known about the position and function of the enzyme's small subunits which were not resolved in the X-ray analysis. We have previously genetically engineered Cys residues into the delta subunit of chloroplast F-1 and used these mutant subunits in cross-linking studies [Lill, H., Hensel, F, Junge, W. & Engelbrecht, S. (1996) J. Biol. Chern. 271, 32737-32742]. In this work, various fluorophores have been introduced into the mutant delta subunits and used in fluorescence-resonance energy-transfer measurements. The resulting distances were fitted into the framework of existing data. Subunit delta was found to be located between two alpha/beta couples, stretching from the level of the nucleotide binding sites up to a position close to the N-termini of subunits alpha and beta. These results corroborate and further refine the previously found location of spinach CF1 delta at the periphery and membrane-distal part of CF1, where it may constitute a part of a stator in the rotatory machinery of F0F1.
ISSN: 00142956
DOI: 10.1046/j.1432-1327.1998.2520277.x

Show full item record

Google ScholarTM

Check

Altmetric