Modification, processing, and subcellular localization in Escherichia coli of the pCloDF13-encoded bacteriocin release protein fused to the mature portion of beta-lactamase.

摘要: Abstract A fusion between the pCloDF13-derived bacteriocin release protein and beta-lactamase was constructed to investigate subcellular localization posttranslational modification of in Escherichia coli. The signal sequence 25 28 amino acid residues mature were fused portion beta-lactamase. hybrid (Mr, 31,588) expressed minicells whole cells possessed full activity. Immunoblotting fractions revealed that is present both cytoplasmic outer membranes E. Radioactive labeling experiments presence or absence globomycin showed modified with a diglyceride fatty acids processed by peptidase II, as murein lipoprotein. results indicated pCloDF13-encoded lipoprotein which associated coli cells.