Induction of bacteriocin production in Lactobacillus sake by a secreted peptide

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 cultu...

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Bibliographic Details
Published in:Journal of Bacteriology 1996-04, Vol.178 (8), p.2232-2237
Main Authors: Eijsink, V G, Brurberg, M B, Middelhoven, P H, Nes, I F
Format: Article
Language:English
Subjects:
Amino Acid Sequence
antimicrobial properties
arn mensajero
arn messager
bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Bacterial Proteins - pharmacology
bacteriocinas
bacteriocine
bacteriocins
Bacteriocins - biosynthesis
Bacteriology
Base Sequence
Biochemistry
Cellular biology
Circular Dichroism
estimulo
expresion genica
expression des genes
gene expression
Gene Expression Regulation, Bacterial
Genes, Bacterial
lactobacillus
Lactobacillus - genetics
messenger rna
Molecular Sequence Data
Peptides
Peptides - chemistry
Peptides - metabolism
Peptides - pharmacology
propiedades antimicrobianas
propriete antimicrobienne
Protein Structure, Secondary
protein synthesis
proteinas
proteine
proteins
secrecion
secretion
sintesis de proteinas
stimuli
stimulus
synthese proteique
Transcription, Genetic
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Summary: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.
ISSN:0021-9193
1098-5530
1067-8832
DOI:10.1128/jb.178.8.2232-2237.1996