Requirement for signal peptide cleavage of Escherichia coli prolipoprotein.
Oligonucleotide-directed site-specific mutagenesis was applied to alter the cleavage site in the signal peptide of the major outer membrane lipoprotein of Escherichia coli. Replacing the glycine residue at the cleavage site with an alanine residue did not affect the processing of the signal peptide. However, when the same cleavage site was constructed by the deletion of the glycine residue, the signal peptide was no longer cleaved. These results indicate that stringent structural integrity at the cleavage site in the lipoprotein signal sequence is required for correct processing of prolipoprotein.
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins; D001483:Base Sequence; D004269:DNA, Bacterial / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008074:Lipoproteins / Q000096:biosynthesis*; D008565:Membrane Proteins / Q000096:biosynthesis; D009154:Mutation; D011498:Protein Precursors / Q000096:biosynthesis*
D001425:Bacterial Outer Membrane Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; D008074:Lipoproteins; C099932:Lpp protein, E coli; D008565:Membrane Proteins; D011498:Protein Precursors