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Accumulation of glyceride‐modified pre‐penicillinase of Bacillus licheniformis in Escherichia coli treated with globomycin
Author(s) -
Hussain Musaddeq,
Oliver Lampen J.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81110-7
Subject(s) - bacillus licheniformis , escherichia coli , biochemistry , cysteine , chemistry , glyceride , bacterial outer membrane , protease , enterobacteriaceae , biology , bacillus subtilis , microbiology and biotechnology , enzyme , bacteria , fatty acid , genetics , gene
The membrane penicillinase of Bacillus licheniformis is a glyceride‐cysteine lipoprotein whose NH 2 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 .