Nine amino acid residues at the NH2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli.
We have examined the structural requirements at the NH2-terminal region of the lipoprotein for its assembly in the outer membrane of Escherichia coli by constructing a hybrid protein consisting of an NH2-terminal portion of the prolipoprotein, consisting of the signal peptide and 9 amino acid residues of lipoprotein, and the entire beta-lactamase sequence. The results from this study indicate that the hybrid protein is modified with glyceride, processed in a globomycin-sensitive step, and localized in the outer membrane. The translocation of the hybrid protein across the cytoplasmic membrane occurs post-translationally and is inhibited by carbonyl cyanide m-chlorophenylhydrazone. Our results, therefore, indicate that the signal peptide and 9 amino acid residues of prolipoprotein are sufficient for its modification, processing, and localization in the outer membrane.
D000595:Amino Acid Sequence; D001483:Base Sequence; D002462:Cell Membrane / Q000378:metabolism; D004269:DNA, Bacterial / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D008074:Lipoproteins / Q000096:biosynthesis* / Q000235:genetics; D014018:Tissue Distribution
D004269:DNA, Bacterial; D008074:Lipoproteins