The role of outer membrane proteins in peptide uptake by Escherichia coli

Abstract The influence of various outer membrane proteins on peptide penetration through the outer membrane in Escherichia coli was assessed by determining peptide transport kinetics in wild type and outer membrane protein-deficient strains. Peptide uptake was measured in whole cells by using a fluorescamine-based assay to monitor continuously the removal of peptides from the medium. Transport data were collected and processed using a microcomputer to give overall K _m and V _max values for peptide transport in each strain. In the mutants, K _m values were changed more markedly then V _max values reflecting an alteration in diffusion through the envelope. This approach shows that porins are involved in facilitating peptide penetration and that the OmpF channel appears to be more important than either OmpC or PhoE proteins. The loss of OmpA protein also decreases outer membrane permeability towards peptides, although whether this protein forms pores itself or exists more to maintain the functional integrity of other proteins is not known.