A colicin A fragment containing the receptor binding domain can be directed to the periplasmic space in E. coli through gene fusion.
The central region of the colicin A polypeptide chain has been fused to the N-terminal part of beta-lactamase through genetic recombination. This region comprising amino acid residues 70-335 confers on the hybrid protein the ability to protect sensitive cells from the lethal action of colicin A. Although colicin A belongs to the cytoplasmic compartment of E. coli, export of the hybrid protein to the periplasmic space was promoted by the signal peptide of beta-lactamase.
D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism*; D003001:Cloning, Molecular; D003087:Colicins / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D010446:Peptide Fragments / Q000235:genetics*; D010455:Peptides / Q000235:genetics; D055503:Protein Multimerization; D021382:Protein Sorting Signals; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic / Q000378:metabolism; D001618:beta-Lactamases / Q000235:genetics
D003087:Colicins; D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D010455:Peptides; D021382:Protein Sorting Signals; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; C028593:colicin receptor, E coli; D001618:beta-Lactamases