F0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c.
Four different sets of proteoliposomes were prepared from F0, subunit c, a complex of subunits a and c (ac complex) and an ac complex supplemented with subunit b. Only liposomes containing intact F0 or all subunits of F0 were active in proton translocation and F1 binding [Schneider, E. and Altendorf, K. (1985) EMBO J. 4, 515-518]. The conformation of subunit c in the different preparations was analyzed by labelling the proteoliposomes with the hydrophobic photoactivatable reagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine ([125I]TID). Subsequent isolation and Edman degradation of this polypeptide revealed distinct radioactive labelling patterns over the entire amino acid sequence. In the F0 complex and in the ac complex subunit c retains a labelling pattern which is related to that found in TID-labelled membrane vesicles of Escherichia coli [Hoppe et al. (1984) Biochemistry 23, 5610-5616]. In the absence of subunit a, considerably more and different amino acid residues of subunit c are modified. The labelling data are discussed in relation to structural aspects of F0 and functional properties of proteoliposomes reconstituted with F0 or individual subunits.
D001389:Azirines / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D008081:Liposomes; D046911:Macromolecular Substances; D011485:Protein Binding; D011510:Proteolipids; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D001389:Azirines; D008081:Liposomes; D046911:Macromolecular Substances; D011510:Proteolipids; C020485:proteoliposomes; C033174:3-(trifluoromethyl)-3-(3-iodophenyl)diazirine; D006180:Proton-Translocating ATPases