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J. Biochem, 1980, Vol. 87, No. 4 1119-1126
© 1980 Japanese Biochemical Society

research-article

Comparative Study on R-type Pyocins of Pseudomonas aeruginosa

Mariko OHSUMI1, Tomoyuki SHINOMIYA and Makoto KAGEYAMA

Mitsubishi-Kasei Institute of Life Sciences Minamiooya, Machida, Tokyo 194

Four R-type pyocins (R1, R2, R3, and R4) produced by different Pseudomonas aeruginosa strains were compared with respect to their structure and action mechanism. It is known that these bacteriocins have structures similar to contractile bacteriophage tails and serologically cross-react with each other, but they are distinguished according to difference in range of sensitive strains. All these pyocins were shown to arrest the synthesis of protein and nucleic acid in sensitive cells, as previously reported for pyocin R1. Action of pyocin R3 was shown to require calcium ion. Although antiserum prepared against one pyocin neutralized other R-type pyocins as well as the homologous pyocin, some differences in antigen specificity were found between pyocin R1 and pyocin R2 or R3 by antibody blocking assays. Electron microscopic observation of pyocin particles treated with the antiserum pre-absorbed with heterologous pyocin revealed that specific antigens were located on the distal portion of the fibers. Comparison of protein composition showed these pyocins to be composed of essentially similar subunit proteins but a subunit protein supposed to be a main constituent of the fiber was different in its molecular weight among these pyocins. These results suggest that the main structural difference of these pyocins is to be found in the fibers.

1Present address: Department of Biochemistry, Faculty of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113.


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