PMID:2863271
| Citation |
Aris, JP, Klionsky, DJ and Simoni, RD (1985) The Fo subunits of the Escherichia coli F1Fo-ATP synthase are sufficient to form a functional proton pore. J. Biol. Chem. 260:11207-15 |
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| 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. |
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| Keywords |
Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology; Cell Membrane/enzymology; Cross-Linking Reagents/pharmacology; DNA Restriction Enzymes; Escherichia coli/enzymology; Escherichia coli/genetics; Kinetics; Macromolecular Substances; Plasmids; Proton-Translocating ATPases/genetics; Proton-Translocating ATPases/metabolism; Species Specificity; Succinimides/pharmacology |
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