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. 1996 Apr;178(8):2232–2237. doi: 10.1128/jb.178.8.2232-2237.1996

Induction of bacteriocin production in Lactobacillus sake by a secreted peptide.

V G Eijsink 1, M B Brurberg 1, P H Middelhoven 1, I F Nes 1
PMCID: PMC177930  PMID: 8636023

Abstract

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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Selected References

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