Biosynthesis and assembly of envelope lipoprotein in a glycerol-requiring mutant of Salmonella typhimurium.

A glycerol-requiring mutant of Salmonella typhimurium was used in a study of the biosynthesis and assembly of a structural lipoprotein in the cell envelope of gram-negative bacteria. Upon removal of glycerol from the growth medium, the biosynthesis of lipoprotein, as measured by radioactive arginine incorporation, was reduced by the same extent as that of other envelope proteins, the cumulative incorporation of arginine being 20% of that of the unstarved control cells. However, the incorporation of radioactive palmitate into lipoprotein was more severely curtailed after glycerol starvation, the cumulative rate of which was 8% of that observed in the unstarved cells. It was further observed that the lipoprotein synthesized in the glycerol-starved cells was more enriched in unmodified cysteine, which is known to be the N-terminal amino acid of lipoprotein, than that synthesized in the unstarved cells. We conclude that the synthesis of the apoprotein portion of Braun's lipoprotein proceeds independently of the attachment of diglyceride to the sulfhydryl group of the N-terminal cysteine and may, in fact, precede the incorporation of the diglyceride moiety.