Calcium ions are involved in Escherichia coli chemotaxis.

Academic Article


  • Escherichia coli regulates intracellular free Ca2+ at about 90 nM [Gangola, P. & Rosen, B. P. (1987) J. Biol. Chem. 262, 12570-12574]. To increase intracellular free Ca2+, nitr-5/Ca2+, a "caged" Ca2+ compound, was electroporated into cells and then its affinity for Ca2+ was reduced by exposure to 370-nm light. Upon release of the Ca2+ ions, the cells tumbled. Studies on mutant strains showed that the receptor proteins (methyl-accepting chemotaxis proteins, MCPs) were not required for the Ca(2+)-induced tumbling but that CheA, CheW, and CheY proteins were required. Similar results were obtained with DM-nitrophen/Ca2+, another caged calcium compound that releases Ca2+ upon illumination at 340 nm. Diazo-2, a caged Ca2+ chelator that takes up Ca2+ upon illumination at 340 nm, was used to decrease intracellular free Ca2+, and this caused smooth swimming.
  • Authors

  • Tisa, Louis
  • Adler, J
  • Status

    Publication Date

  • December 15, 1992
  • Keywords

  • Bacterial Proteins
  • Calcium
  • Chemotactic Factors
  • Chemotaxis
  • Cytoplasm
  • Escherichia coli
  • Escherichia coli Proteins
  • Histidine Kinase
  • Membrane Proteins
  • Methyl-Accepting Chemotaxis Proteins
  • Digital Object Identifier (doi)

    Start Page

  • 11804
  • End Page

  • 11808
  • Volume

  • 89
  • Issue

  • 24