In vitro membrane association of the F0 polypeptides of the Escherichia coli proton translocating ATPase.
The F0 polypeptides a, b, and c of the H+-translocating ATPase associated with membranes when synthesized in vitro. This association occurred when the membranes were present either cotranslationally or post-translationally. In addition, the F0 polypeptides associated with liposomes. The membrane association seemed to be an insertion process since there was protection of polypeptides a and c from proteolysis. The in vitro insertion of the F0 polypeptides a, b, and c was independent of the synthesis of each polypeptide and of the F1 polypeptides.
D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000302:isolation & purification; D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology*; D005796:Genes; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000235:genetics*; D008970:Molecular Weight; D006180:Proton-Translocating ATPases
D046911:Macromolecular Substances; D008565:Membrane Proteins; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases