Final steps of the maturation of Omp F, a major protein from the outer membrane of Escherichia coli.
Pulse-labelling experiments with E. coli cells allowed us to follow the incorporation of de novo proteins into the outer membrane of the cell envelope. Labelled membrane samples containing increasingly different levels of newly synthesized Omp F protein were subjected to chemical cross-linking with a bifunctional cleavable reagent in order to investigate the process of trimer formation of the protein. From the results obtained, we conclude that the formation of functional Omp F trimers is substantially delayed to, and can be distinguished from, the incorporation of Omp F monomers to the outer membrane.
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D007096:Imidoesters / Q000494:pharmacology; D046911:Macromolecular Substances
D001425:Bacterial Outer Membrane Proteins; D003432:Cross-Linking Reagents; D007096:Imidoesters; D046911:Macromolecular Substances; C005905:methyl 4-mercaptobutyrimidate