Abstract
Enterococcus faecalis, a gram-positive bacterium frequently involved in opportunistic infections and antibiotic resistances, produces a family of oligopeptide signaling molecules as bacterial sex pheromones. Conjugative transfer of a bacteriocin plasmid pPD1 is activated by a peptide pheromone cPD1 ( NH 2– Phe–Leu–Val–Met–Phe–Leu–Ser–Gly–OH) secreted from pPD1-free recipient bacteria (1) and is blocked by an oligopeptide inhibitor iPD1 (NH 2–Ala–Leu– Ile–Leu–Thr–Leu–Val–Ser–OH) secreted from pPD1-carrying donor bacteria (2). In this study, we investigated how pPD1-carrying bacterial cell receives these peptide signals using a tritiated pheromone, [3H]cPD1.
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