Publication | Open Access
Enterococcus faecalis pheromone binding protein, PrgZ, recruits a chromosomal oligopeptide permease system to import sex pheromone cCF10 for induction of conjugation.
182
Citations
27
References
1996
Year
Environmental SignalingProtein SecretionMicrobial PathogensBacteriologyMolecular BiologyBacterial PathogensSex Pheromone Ccf10Peptide Sex PheromoneProteomicsIntercellular CommunicationHost-pathogen InteractionsVirulence FactorMolecular MicrobiologyClinical MicrobiologyPlasmid Pcf10Signal TransductionNatural SciencesPathogenesisBiological FunctionMicrobiologyConjugative TransferSystems BiologyMedicine
Conjugative transfer of the plasmid pCF10 by Enterococcus faecalis donor cells occurs in response to a peptide sex pheromone, cCF10, secreted by recipients. The plasmid-encoded cCF10 binding protein, PrgZ, is similar in sequence to binding proteins (OppAs) encoded by oligopeptide permease (opp) operons. Mutation of prgZ decreased the sensitivity of donor cells to pheromone, whereas inactivation of the chromosomal E. faecalis opp operon abolished response at physiological concentrations of pheromone. Affinity chromatography experiments demonstrated the interaction of the pheromone with several putative intracellular regulatory molecules, including an RNA molecule required for positive regulation of conjugation functions. These data suggest that processing of the pheromone signal involves recruitment of a chromosomal Opp system by PrgZ and that signaling occurs by direct interaction of internalized pheromone with intracellular effectors.
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