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J. Bacteriol., Apr 1996, 2232-2237, Vol 178, No. 8
Copyright © 1996, American Society for Microbiology

Induction of bacteriocin production in Lactobacillus sake by a secreted peptide

VG Eijsink, MB Brurberg, PH Middelhoven and IF Nes
Laboratory of Microbial Gene Technology, Department of Biotechnological Sciences, Agricultural University of Norway, As.

Lactobacillus sake LTH673 is known to produce a bacteriocin called sakacin P. Production of and immunity to sakacin P were found to depend on the presence of a protease-sensitive component that is produced by L. sake LTH673 itself. This component (called inducing factor [IF]) was purified from culture supernatants and shown to be a basic, nonbacteriocin peptide consisting of 19 amino acids, which in principle is capable of forming a highly amphiphilic helical structure. Circular dichroism studies showed that IF indeed could adopt a helical structure, but only in membrane-mimicking environments. Both purified IF and chemically synthesized IF induced expression of the structural gene for sakacin P and concomitant secretion of the gene product. In addition, IF induced its own production and immunity to sakacin P and related bacteriocins. These results indicate that bacteriocin production by L. sake LTH673 is controlled by an autoinduction pathway in which IF may function as a cell density signal.


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