The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis

Mol Microbiol. 2003 Mar;47(5):1353-66. doi: 10.1046/j.1365-2958.2003.03375.x.


Escherichia coli cells use two distinct sensory circuits during chemotaxis towards carbohydrates. One circuit requires the phosphoenolpyruvate-dependent phosphotransferase system (PTS) and is independent of any specific chemoreceptor, whereas the other uses a chemoreceptor-dependent sensory mechanism analogous to that used during chemotaxis towards amino acids. Work on the carbohydrate chemotaxis sensory circuit of Bacillus subtilis reported in this article indicates that the B. subtilis circuit is different from either of those used by E. coli. Our chemotactic analysis of B. subtilis strains expressing various chimeric chemoreceptors indicates that the cytoplasmic, C-terminal module of the chemoreceptor McpC acts as a sensory-input element during carbohydrate chemotaxis. Our results also indicate that PTS-mediated carbohydrate transport, but not carbohydrate metabolism, is required for production of a chemotactic signal. We propose a model in which PTS-transport-induced chemotactic signals are transmitted to the C-terminal module of McpC for control of chemotaxis towards PTS carbohydrates.

Publication types

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

MeSH terms

  • Bacillus subtilis / chemistry
  • Bacillus subtilis / drug effects*
  • Bacillus subtilis / physiology
  • Bacterial Proteins*
  • Carbohydrate Metabolism
  • Carbohydrates / pharmacology*
  • Chemotaxis / drug effects
  • Chemotaxis / physiology*
  • Cytoplasm / metabolism
  • Escherichia coli / physiology
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Methyl-Accepting Chemotaxis Proteins
  • Models, Molecular
  • Phosphoenolpyruvate Sugar Phosphotransferase System / physiology
  • Protein Conformation
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / metabolism
  • Signal Transduction / physiology
  • Species Specificity
  • Structure-Activity Relationship


  • Bacterial Proteins
  • Carbohydrates
  • Membrane Proteins
  • Methyl-Accepting Chemotaxis Proteins
  • Recombinant Fusion Proteins
  • Phosphoenolpyruvate Sugar Phosphotransferase System