Assembly of a functional F0 of the proton-translocating ATPase of Escherichia coli.
We have investigated both structural and functional assembly of the F0 portion of the Escherichia coli proton-translocating ATPase in vivo. Fractionation of E. coli minicells containing plasmids which code for parts of the unc operon shows that each of the F0 peptides a, b, and c insert into the cytoplasmic membrane independent of each other and without the polypeptides which form the F1 portion of the complex alpha, beta, gamma, delta, and epsilon. Assays of membrane energization indicate that, while formation of a functional proton channel requires the presence of all three F0 polypeptides a, b and c, they are not sufficient. Synthesis of both the alpha and beta subunits of the F1 are required for formation of a functional proton channel.
D000251:Adenosine Triphosphatases / Q000032:analysis* / Q000235:genetics; D004262:DNA Restriction Enzymes / Q000378:metabolism; D004579:Electron Transport; D004734:Energy Metabolism; D004926:Escherichia coli / Q000201:enzymology*; D005453:Fluorescence; D046911:Macromolecular Substances; D009876:Operon; D010957:Plasmids; D006180:Proton-Translocating ATPases
D046911:Macromolecular Substances; D004262:DNA Restriction Enzymes; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases