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.[1]References
- Characterization of a novel lipoprotein mutant in Escherichia coli. Giam, C.Z., Hayashi, S., Wu, H.C. J. Biol. Chem. (1984) [Pubmed]
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