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SUMMARY: Serratia marcescens strain HY was found to produce marcescin B in addition to the production of marcescin A which was already known. The synthesis of both marcescins was inducible by mitomycin C, but A was induced much less than B. Both marcescins were isolated from the culture fluid of a mutant deficient in exocellular protease, and purified by ammonium sulphate precipitation, gel-filtration, and ion-exchange chromatography on hydroxylapatite and DEAE-cellulose. Marcescin A has a molecular weight of 2 x 106, is resistant to trypsin, attacks some S. marcescens as well as Escherichia coli strains, and its mode of action resembles, in many respects, that of colicin E2, i.e. it inhibits the synthesis of DNA, RNA and protein in sensitive cells and, furthermore, causes degradation of DNA: at high concentrations it also degrades RNA. Marcescin B, on the other hand, has a low molecular weight (43000), is sensitive to trypsin, does not act on S. marcescens strains, and its mode of action seems to be similar to that of colicin EI, i.e. it inhibits the synthesis of DNA, RNA and protein in sensitive cells without DNA-degradation. Thus, several properties of the two marcescins produced by strain HY agree well with the (few) data already published on marcescins derived from other strains. The synthesis of marcescin B resembles that of marcescin A as regards the pleiotropic effect of nucsu mutations.

Purification and Mode of Action of Two Bacteriocins Produced by Serratia marcesens HY