Purification of the pyocin S2 complex from Pseudomonas aeruginosa PAO1: analysis of DNase activity.
Pyocin S2 purified from mitomycin C-induced lysates of Pseudomonas aeruginosa strain PAO1 has been shown to consist of a complex of two proteins. Further analysis of the purified S2 complex revealed that the 74 kd S2 pyocin demonstrates DNase activity which can be blocked by S2-specific antisera. Chromosomal DNA from pyocin sensitive cells treated with the pyocin S2 complex in vitro did not show any degradation, suggesting that the 10 kd protein inhibits the DNase activity of the S2 protein. These results suggest an alternative mechanism for the toxicity associated with the S2 pyocin.
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Department of Microbiology, Ohio State University, Columbus 43210-1292.
Galloway
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D000911:Antibodies, Monoclonal; D003851:Deoxyribonucleases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D011550:Pseudomonas aeruginosa / Q000187:drug effects / Q000201:enzymology / Q000254:growth & development*; D011709:Pyocins / Q000302:isolation & purification* / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D011709:Pyocins; D003851:Deoxyribonucleases