Isolation and structure of bacterial sex pheromone, cPD1

Science. 1984 Nov 16;226(4676):849-50. doi: 10.1126/science.6436978.

Abstract

The Streptococcus faecalis sex pheromone cPD1, which induces a mating response in cells harboring the conjugative plasmid pPD1, has been isolated and its structure determined. It was found to have a molecular weight of 912, and its amino acid sequence was H-Phe-Leu-Val-Met-Phe-Leu-Ser-Gly-OH. A synthetic octapeptide showed the same biological activity and chromatographic behavior as the isolated cPD1. Pheromone activity was detectable at a concentration of approximately 4 X 10(-11)M.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Enterococcus faecalis / physiology*
  • Oligopeptides / isolation & purification*
  • Pheromones / isolation & purification*
  • Plasmids
  • Sex Attractants / isolation & purification*

Substances

  • Oligopeptides
  • Pheromones
  • Sex Attractants
  • Streptococcus faecalis sex pheromone cPD1