Acetyladenylate plays a role in controlling the direction of flagellar rotation.
- 1 September 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (18), 6711-6715
- https://doi.org/10.1073/pnas.85.18.6711
Abstract
Cells of Escherichia coli deleted for genes that code for the transducers and all the known cytoplasmic Che proteins except CheY responded reversibly to the addition of acetate by spinning their flagellar motors clockwise. By varying growth conditions and using metabolic inhibitors and mutants deficient in acetate metabolism, this effect was shown to require acetate-CoA synthetase [acetate:CoA ligase (AMP-forming); EC 6.2.1.1], an enzyme that catalyzes the formation of acetyl-CoA from acetate by an acetyladenylate intermediate. A mutant deficient in this enzyme but retaining the chemotaxis genes was deficient for chemotaxis. Thus, acetyladenylate appears to play a role in generating clockwise rotation at the level of CheY or the motor.Keywords
This publication has 31 references indexed in Scilit:
- CheA protein, a central regulator of bacterial chemotaxis, belongs to a family of proteins that control gene expression in response to changing environmental conditions.Proceedings of the National Academy of Sciences, 1988
- Sensory transduction in bacterial chemotaxis involves phosphotransfer between CHE proteinsBiochemical and Biophysical Research Communications, 1988
- Conserved domains in bacterial regulatory proteins that respond to environmental stimuliCell, 1987
- Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coliJournal of Bacteriology, 1987
- Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimuriumJournal of Bacteriology, 1986
- Restoration of flagellar clockwise rotation in bacterial envelopes by insertion of the chemotaxis protein CheY.Proceedings of the National Academy of Sciences, 1986
- Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli.Proceedings of the National Academy of Sciences, 1986
- The role of a signaling protein in bacterial sensing: behavioral effects of increased gene expression.Proceedings of the National Academy of Sciences, 1984
- Requirement of ATP in bacterial chemotaxis.Journal of Biological Chemistry, 1982
- A Method for Measuring Chemotaxis and Use of the Method to Determine Optimum Conditions for Chemotaxis by Escherichia coliJournal of General Microbiology, 1973