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. 1976 Sep;127(3):1494–1501. doi: 10.1128/jb.127.3.1494-1501.1976

Novel mutation that causes a structural change in a lipoprotein in the outer membrane of Escherichia coli.

H Suzuki, Y Nishimura, H Iketani, J Campisi, A Hirashima
PMCID: PMC232945  PMID: 783146

Abstract

A novel mutation which caused a structural change in a lipoprotein in the outer-membrane has been found in Escherichia coli K-12. The lipoprotein of the wild-type strain is known to have a peculiar amino terminal structure: glycerylcysteine with two fatty acids attached by ester linkages and one fatty acid by an amide linkage. In contrast to the wild-type lipoprotein, the mutant lipoproteins is isolated from the E. coli envelope as a dimer of molecular weight of about 15,000. The dimer can be reduced by mercaptoethanol to the lipoprotein monomer of molecular weight of about 7,500. The monomer has a free thiol group which is susceptible to monoiodacetie mutant lipoprotein is extremely low in comparison with that into the wild-type lipoprotein. These results suggest that the mutant is defective in transferring a glycerol group to the thiol group of the amino terminal cysteine residue of the lipoprotein. The gene responsible for this modification reaction has been located at 36.5 min on the E. coli chromosome.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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