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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Dec 15;89(24):11804–11808. doi: 10.1073/pnas.89.24.11804

Calcium ions are involved in Escherichia coli chemotaxis.

L S Tisa 1, J Adler 1
PMCID: PMC50645  PMID: 1465403

Abstract

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.

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Selected References

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