Expression of Bacillus cereus hemolysin II in Bacillus subtilis renders the bacteria pathogenic for the crustacean Daphnia magna.

Hemolysin II (HlyII) is a pore-forming toxin of the opportunistic pathogen Bacillus cereus. Despite our understanding of the mechanism of HlyII cytotoxicity in vitro, many of its characteristics, including potential target cells, conditions of its action and expression, are not known. Here we report that the expression of hlyII in Bacillus subtilis renders the bacteria hemolytic and is able to kill the crustacean Daphnia magna.

Structural plasmid evolution as a result of coupled recombinations at bom and cer sites.

We have studied the recombination of plasmids bearing bom and cer sites. The bom ( basis of mobilization) site is required for conjugative transfer, while the cer ( Col E1 resolution) site is involved in the resolution of plasmid multimers, which increases plasmid stability. We constructed a pair of parent plasmids in such a way as to allow us select clones containing recombinant plasmids directly.

Characterization of pECL18 and pKPN2: a proposed pathway for the evolution of two plasmids that carry identical genes for a Type II restriction-modification system.

The primary structures of the plasmids pECL18 (5571 bp) and pKPN2 (4196 bp) from Escherichia coli and Klebsiella pneumoniae, respectively, which carry genes for a Type II restriction-modification system (RMS2) with the specificity 5'-CCNGG-3', were determined in order to elucidate the structural relationship between them. The data suggest a possible role for recombination events at bom (basis of mobility) regions and the sites of resolution of multimer plasmid forms (so-called cer sequences) in the structural evolution of multicopy plasmids. Analysis of the sequences of pECL18 and pKPN2 showed that the genes for RM* Ecl18kI and RM* Kpn2kI, and the sequences of the rep (replication) regions in the two plasmids, are almost identical.

Effects of Cryptococcus humicola killer toxin upon Cryptococcus terreus envelope: combined fluorometric and microscopic studies.

Killer toxin (microcin) produced by Cryptococcus humicola 9-6 induced interaction of the fluorogenic dyes, ethidium bromide, propidium iodide, and hemimagnesium 8-anilino-1-naphtalenesulfonate, with the sensitive strain of Cryptococcus terreus VKM Y-2253. The toxin also made the cells susceptible to cetyltrimethylammonium bromide and leaky for K+. When excited at 360 nm, cell-bound ethidium (propidium) fluorescence was enhanced by 8-anilino-1-naphtalensulfonate, and cell-bound 8-anilino-1-naphtalensulfonate fluorescence was quenched by ethidium (propidium), indicating energy transfer from 8-anilino-1-naphtalensulfonate to ethidium (propidium).