Biosynthesis of the covalently linked diglyceride in murein lipoprotein of Escherichia coli.

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Abstract
Biosynthesis of the diglyceride moiety of murein lipoprotein in E. coli was studied by pulse-labeling with [2-3H]glycerol and subsequent chase. The precursor of the glycerol moiety in lipoprotein is probably one of the major phospholipid species in E. coli. Studies of biosynthesis of lipoprotein in cerulenin-treated cells indicated that the nonacylated glycerol moiety of phosphatidylglycerol is the donor for the formation of a thioether linkage in the glycerylcysteine residue of the lipoprotein. This is supported by the observation that C 1 rather than C 3 of sn-glycerol is involved in this thioether linkage. The biosynthesis of lipoprotein apparently proceeds as follows: apolipoprotein + phosphatidylglycerol or acyl phosphatidylglycerol .fwdarw. lipoprotein + phosphatidic acid.