Accumulation of glyceride-modified pre-penicillinase of Bacillus licheniformis in Escherichia coli treated with globomycin.
The membrane penicillinase of Bacillus licheniformis is a glyceride-cysteine lipoprotein whose NH2 terminus is analogous to the major outer membrane lipoprotein of Escherichia coli. When E. coli cells producing B. licheniformis penicillinase were treated with the antibiotic, globomycin, a precursor of the penicillinase, pre-penicillinase, accumulated in the cell. It could be immunoprecipitated with anti-penicillinase antibodies; it contained palmitate; and one of its two cysteine residues was modified by glycerol. The action of globomycin, probably indirectly, also activates protease which acts differently on the pre-penicillinase than does the signal peptidase. The results strongly indicate that the pre-penicillinase is processed by the globomycin-sensitive signal peptidase in E. coli, and the modification of precursor by lipid precedes removal of the signal peptide as it does with the membrane lipoproteins of E. coli.
D000900:Anti-Bacterial Agents; D001407:Bacillus / Q000201:enzymology; D055598:Chemical Phenomena; D002621:Chemistry; D004792:Enzyme Precursors / Q000378:metabolism*; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology; D005989:Glycerides / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D010405:Penicillinase / Q000378:metabolism*; D010455:Peptides / Q000494:pharmacology; D013329:Structure-Activity Relationship; D001618:beta-Lactamases / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D004792:Enzyme Precursors; D005989:Glycerides; D008565:Membrane Proteins; D010455:Peptides; C017339:globomycin; D010405:Penicillinase; D001618:beta-Lactamases