title: The Fo subunits of the Escherichia coli F1Fo-ATP synthase are sufficient to form a functional proton pore.
abstract: The assembly of the Fo sector of the Escherichia coli ATP synthase has been studied using both structural and functional criteria for assembly. Cross-linking E. coli minicell membranes containing only the Fo subunits a, b, and c with dithiobis(succinimidyl propionate) (DSP) produces b2 and c2 dimers that are generated by cross-linking membranes containing the assembled holoenzyme. Five plasmids carrying the genes specifying the Fo polypeptides in a bacterial strain lacking all of the unc (ATP synthase) genes show a good correlation between Fo function and the amount of the membrane-bound Fo polypeptides. In this report we revise a conclusion reached previously (Klionsky, D.J., Brusilow, W.S.A., and Simoni, R.D. (1983) J. Biol. Chem. 258, 10136-10143) and present evidence that the Fo subunits alone are sufficient to assemble a functional proton pore.
authors.forename: J P
authors.initials: JP
authors.lastname: Aris
authors.forename: D J
authors.initials: DJ
authors.lastname: Klionsky
authors.forename: R D
authors.initials: RD
authors.lastname: Simoni
mesh_terms: D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D007700:Kinetics; D046911:Macromolecular Substances; D010957:Plasmids; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D013045:Species Specificity; D013388:Succinimides / Q000494:pharmacology
chemical_list: D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D013388:Succinimides; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D004262:DNA Restriction Enzymes; D006180:Proton-Translocating ATPases; C011240:dithiobis(succinimidylpropionate)