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A mutant of E. coli lacking a specific outer membrane lipoprotein was found. Both the free and the bound form have been lost in this mutant. No material that cross-reacted with antiserum against lipoprotein was detected by the Ouchterlony test. The mutant was defective in producing mRNA active for lipoprotein synthesis. The mutation leading to the loss of lipoprotein synthesis, referred to as lpo, seems to have arisen during production of an F'. The map position of lpo was at 36.5 min on the E. coli K12 map, in the order man, uidA, lpo, aroD, pps. The lpo mutant grew and divided normally and remained susceptible to bacteriophages lambda, phi80, P1, P2, the T series, and f1, f2, and MS2 in its male derivatives. The mutant was hypersensitive to EDTA and cationic dves and somewhat sensitive to detergents. There was considerable leakage of periplasmic enzymes but passive transport of beta-galactoside was unchanged. These physiological characteristics of the mutant suggest that lipoprotein is involved in maintaining the integrity of the outer envelope structure, by bridging the outer membrane and murein, but not in the vital processes of growth and division.

On the process of cellular division in Escherichia coli: a mutant of E. coli lacking a murein-lipoprotein.