A new colicin that adsorbs to outer-membrane protein Tsx but is dependent on the tonB instead of the tolQ membrane transport system.
A new colicin, Col5, was synthesized by an Escherichia coli isolate of human origin from the ECOR Collection. It was unique because it adsorbed to the outer-membrane protein Tsx, but used the tonB rather than the tolQ membrane transport system, which is employed by the only other Tsx-specific colicin, ColK. Col5 was encoded by a 5.2 kb plasmid, p5. It was inducible by mitomycin C, and strains harbouring p5 exhibited quasi-lysis. The bactericidal protein had an M(r) of 56,000.
Bradley
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Faculty of Medicine, Memorial University of Newfoundland, St John's, Canada.
Howard
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SP
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D003086:Bacteriocin Plasmids / Q000235:genetics; D001692:Biological Transport; D003087:Colicins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000378:metabolism*; D011991:Receptors, Virus
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D003087:Colicins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D011991:Receptors, Virus; C057616:tonB protein, Bacteria; C489181:tonB protein, E coli; C060792:tolQ protein, E coli; C066743:Tsx protein, E coli