Biochemical and genetic characterization of a competence pheromone from B. subtilis

Cell. 1994 Apr 22;77(2):207-16. doi: 10.1016/0092-8674(94)90313-1.


We have purified and characterized a modified peptide pheromone that accumulates in culture medium as B. subtilis grows to high density. This pheromone is required for the development of genetic competence. When added to cells at low density, the pheromone induces the premature development of competence. The peptide moiety of the pheromone matches nine of the last ten amino acids predicted from a 55 codon open reading frame, comX. comX and comQ, the gene immediately upstream of comX, are required for production of the pheromone. Response to the pheromone requires the comP-comA two-component regulatory system and the oligopeptide permease encoded by spo0K. Spo0K could transport the pheromone into the cell, or function as a receptor, binding the pheromone and sending a transmembrane signal, leading to activation of the ComA transcription factor and induction of competence development.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / chemistry*
  • Bacillus subtilis / genetics
  • Bacillus subtilis / growth & development
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / isolation & purification
  • Base Sequence
  • Cloning, Molecular
  • Gene Expression Regulation, Bacterial / genetics
  • Genes, Bacterial / genetics*
  • Genes, Regulator / genetics
  • Models, Biological
  • Molecular Sequence Data
  • Mutagenesis
  • Open Reading Frames / genetics
  • Peptide Synthases / genetics
  • Peptides / chemistry
  • Peptides / genetics*
  • Peptides / isolation & purification
  • Signal Transduction / genetics
  • Spores, Bacterial / genetics
  • Transformation, Bacterial


  • Bacterial Proteins
  • ComX protein, Bacillus subtilis
  • Peptides
  • Peptide Synthases
  • surfactin synthetase