Open AccessIn vitro membrane association of the F0 polypeptides of the Escherichia coli proton translocating ATPase
Author(s) -
Karl Decker,
William S.A. Brusilow,
Robert P. Gunsalus,
Robert D. Simoni
Publication year - 1982
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.152.2.815-821.1982
Subject(s) - biology , in vitro , proteolysis , membrane , atpase , escherichia coli , biochemistry , membrane protein , microbiology and biotechnology , enzyme , gene
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.