A colicin A fragment containing the receptor binding domain can be directed to the periplasmic space in E. coli through gene fusion
- 9 July 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 172 (2), 183-188
- https://doi.org/10.1016/0014-5793(84)81122-9
Abstract
The central region of the colicin A polypeptide chain has been fused to the N-terminal part of β-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 β-lactamaseKeywords
This publication has 23 references indexed in Scilit:
- Complete nucleotide sequence of the structural gene for colicin A, a gene translated at non-uniform rateJournal of Molecular Biology, 1983
- Variable rate of polypeptide chain elongation for colicins A, E2 and E3Journal of Molecular Biology, 1982
- Physical map of pColA-CA31, an amplifiable plasmid, and location of colicin a structural geneGene, 1982
- Involvement of BtuB and OmpF proteins in binding and uptake of colicin AFEMS Microbiology Letters, 1981
- Secretion into the bacterial periplasmic space of chicken ovalbumin synthesized in Escherichia coliGene, 1981
- Exclusive Localization of Colicin A in Cell Cytoplasm of Producing BacteriaEuropean Journal of Biochemistry, 1981
- Biosynthesis and Export of Colicin A inCitrobacter freundiiCA31European Journal of Biochemistry, 1981
- Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragmentsBiochemistry, 1980
- Limited proteolysis of cloacin DF13 and characterization of the cleavage productsBiochemistry, 1978
- Antibodies as probes for detection of conformational changes in proteins. A model study with the alkaline phosphatase of Escherichia coliJournal of Molecular Biology, 1975