CheA, CheW, and CheY are required for chemotaxis to oxygen and sugars of the phosphotransferase system in Escherichia coli
Open Access
- 1 October 1995
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 177 (20) , 6011-6014
- https://doi.org/10.1128/jb.177.20.6011-6014.1995
Abstract
We carried out studies with Escherichia coli to determine the site at which the methylation-independent pathways for taxis to oxygen and to sugars of the phosphoenolpyruvate:sugar phosphotransferase transport system converge with the methylation-dependent chemotaxis pathways. Using genetic reconstitution of the pathways in a null strain, we determined that all pathways examined required the products of the genes cheA, cheW, and cheY. Thus, we conclude that both the methylation-independent and methylation-dependent pathways converge at CheA, the histidine kinase product of cheA.Keywords
This publication has 14 references indexed in Scilit:
- Universal Themes of Signal Transduction in BacteriaPublished by Elsevier ,1993
- SIGNAL TRANSDUCTION PATHWAYS INVOLVING PROTEIN PHOSPHORYLATION IN PROKARYOTESAnnual Review of Biochemistry, 1991
- Signal transduction in chemotaxis to oxygen in Escherichia coli and Salmonella typhimuriumJournal of Bacteriology, 1988
- Signaling Pathways in Bacterial ChemotaxisBotanica Acta, 1988
- Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coliJournal of Bacteriology, 1987
- Inversion of aerotactic response in Escherichia coli deficient in cheB protein methylesteraseJournal of Bacteriology, 1986
- Oxygen taxis and proton motive force in Salmonella typhimurium.Journal of Biological Chemistry, 1984
- ROLE OF PROTON MOTIVE FORCE IN SENSORY TRANSDUCTION IN BACTERIAAnnual Review of Microbiology, 1983
- Novel sensory adaptation mechanism in bacterial chemotaxis to oxygen and phosphotransferase substrates.Proceedings of the National Academy of Sciences, 1982
- Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system.Proceedings of the National Academy of Sciences, 1977