학술논문
Deletion of internal twenty‐one amino acid residues of Escherichia coliprolipoprotein does not affect the formation of the murein‐bound lipoprotein
Document Type
Article
Author
Source
FEBS Letters; October 1992, Vol. 311 Issue: 3 p311-314, 4p
Subject
Language
ISSN
00145793
Abstract
Mutation pgsAaffecting the phosphatidylglycerol phosphate synthesis is lethal for all but certain E. colistrains such as strains deleted for the lppgene or strains containing unmodifiable prolipoprotein like lppD14. Strain SD312 pgsA3 is tolerant to pgsAmutation, which suggests the lppalleles in strain SD312 pgsA3 and its parental strain SD12 may be defective. DNA sequence analysis of the lppgenes in Escherichia colistrains SD12 and SD312 pgsAusing asymmetric polymerase chain reaction showed that the lppalleles in these two strains contained a 63 base pair deletion corresponding to the 37th to 57th codons of the wild‐type lppgene. [3H]Palmitate labeling of strains SD12 and SDS312 showed that the mutant lipoprotein in SD12 strain was modified with lipid, while the prolipoprotein in SD312 was not modified. The shortened mature lipoprotein in SD12 and the lipid‐modified prolipoprotein in globomycin‐treated SD12 were found to be covalently attached to the peptidoglycan, while the unmodified prolipoprotein in SD312 did not form significant amounts of murein‐bound lipoprotein.