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Bacteriocins, Microcins and Lantibiotics by Roberto Kolter, Felipe Moreno (auth.), Richard James, Claude

By Roberto Kolter, Felipe Moreno (auth.), Richard James, Claude Lazdunski, Franc Pattus (eds.)

Awarded listed here are contemporary findings on bacteriocins: plasmid-encoded pollutants produced by way of micro organism, which fluctuate from conventional antibiotics in killing simply micro organism which are heavily regarding the manufacturing pressure. incorporated are introductory chapters on bacteriocins, microcins (low molecular weight bacteriocins), and lantibiotics (peptide antibiotics containing lanthionine), extra, contributions on pore forming bacteriocins, the mechanisms of immunity to bacteriocins, uptake and secretion, in addition to evolution of bacteriocins. it really is of specific curiosity that the lantibiotic nisin is licensed to be used as nutrition preservative and one other lantibiotic, epidermin, has power as a healing drug opposed to zits.

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These results strongly support the presence of a ring structure chromophore in MccB 17. The fmal structural infonnation we present comes from two-dimensional NMR spectra ofMccB 17. The most unexpected result from these data is that forty-two distinct amide protons have been identified. This indicates that in DMSO MccB 17 possesses a highly ordered structure, despite its high glycine content. Even the three N-tenninal and three C-tenninal residues of the protein are sufficiently ordered to have been identified and structurally defmed in the spectra, results which are unexpected for any protein.

Delbrueckii. This bacteriocin was selected for further molecular analysis in our laboratory since it was unique relative to other bacteriocins of lactic acid bacteria (Joerger & Klaenhammer, 1986, 1990). , 1984) and immunoscreening of the library with polyclonal antibodies specific for the bacteriocin (Joerger & Klaenhammer, 1990). Two recombinant phage produced he1veticin J-lacZ fusion proteins and contained DNA inserts of 350 and 600 bp which were homologous to each other and specific for the strain producing he1veticin J.

A strain containing the mcbA gene alone and strains containing mutations in either mcbB, mcbC, or mcbD were labeled with 3H-glycine and compared to a wild-type MccB 17-producing strain. Half of each labeled sample was run as total protein (Figure 1, top panel) while the other half was immunoprecipitated with anti-MccB 11 polyclonal antibodies (Figure 7, bottom panel). Polyclonal antibodies raised against mature MccBI7, which immunoprecipitated proMccBl7, do not recognize the precursor nor any of the comigrating bands from the mcbB, C and D mutants.

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