Mechanism of export of outer membrane lipoproteins through the cytoplasmic membrane in Escherichia coli. Binding of lipoprotein precursors to the peptidoglycan layer.

Upon treatment of Escherichia coli cells with globomycin, precursors of Braun's lipoprotein, a peptidoglycan-associated lipoprotein (PAL) and several new species of lipoproteins accumulated in the cell envelope (Hussain, M. Ichihara, S., and Mizushima, S. (1980) J. Biol. Chem. 255, 3707-3012; and Ichihara, S., Hussain, M., and Mizushima, S. (1981) J. Biol. Chem. 256, 3125-3129). The precursors of the Braun's lipoprotein and PAL thus accumulated were able to interact with the peptidoglycan layer. A considerable fraction of the precursor of Braun's lipoprotein was covalently bound to the peptidoglycan layer through its COOH-terminal lysine residue in the same manner as in the mature form. The manner of interaction of the precursor of PAL with the peptidoglycan layer was also the same as that of its mature form in which the central to COOH-terminal region of the lipoprotein is important for the interaction. Both precursors were localized in the cytoplasmic membrane when the outer and cytoplasmic membranes were separated after digestion by lysozyme of the peptidoglycan layer. When the cell envelope fraction was incubated, these precursors were chased to the corresponding mature forms. These results indicate that these proteins can be exported through the cytoplasmic membrane while they still retain the signal peptide that is most probably held in the cytoplasmic membrane.