Characterization of a novel lipoprotein mutant in Escherichia coli.
Mutants altered in the structural gene for murein lipoprotein in Escherichia coli can be isolated by globomycin selection. We have isolated a unique globomycin-resistant mutant, strain 6-23, which synthesizes a structurally altered, albeit modified and processed, lipoprotein. DNA sequence analysis of the mutant lpp allele and determination of the amino acid composition of the mutant lipoprotein revealed a single amino acid substitution of cysteine for arginine at the 68th amino acid residue of prolipoprotein. Pulse-chase experiments revealed that the kinetics of lipoprotein maturation was affected by this alteration in the structure of lipoprotein.
D000483:Alleles; D000595:Amino Acid Sequence; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005796:Genes; D005798:Genes, Bacterial; D007700:Kinetics; D008074:Lipoproteins / Q000235:genetics*; D009154:Mutation; D010457:Peptidoglycan / Q000235:genetics*; D010957:Plasmids; D013045:Species Specificity
D008074:Lipoproteins; D010457:Peptidoglycan