Accumulation of glyceride‐modified pre‐penicillinase of Bacillus licheniformis in Escherichia coli treated with globomycin

FEBS Letters

Hussain, Musaddeq¹  Oliver Lampen, J.¹ 

[1] Waksman Institute of Microbiology, Rutgers University, PO Box 759, Piscataway, NJ 08854, USA

关键词: Pre-penicillinase;    Bacillus licheniformis;    Escherichia coli;    Globomycin;    Lipid modification;    Signal peptidase;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(83)81110-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown