Temperature-sensitive processing of outer membrane lipoprotein in an Escherichia coli mutant.
A mutant of Escherichia coli that accumulated prolipoprotein, a secretory precursor of the outer membrane lipoprotein, was isolated. The prolipoprotein accumulated in this mutant was modified by glyceride, but the in vitro cleavage of the signal peptide of the accumulated prolipoprotein was found to be temperature sensitive. The mutation appears to be located outside the gene for the lipoprotein, thus suggesting that the gene for the signal peptidase for the prolipoprotein was mutated.
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000378:metabolism*; D010450:Endopeptidases / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D008074:Lipoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D009154:Mutation; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases; D013696:Temperature
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008074:Lipoproteins; D008565:Membrane Proteins; D011498:Protein Precursors; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase