Locations of Mapped Genes:
Synonyms: Energy taxis signal transduction, Redox taxis signal transduction
|Superclasses:||Signal transduction pathways|
Energy taxis is the ability of bacteria to monitor their internal energy levels and respond by moving to a position that is optimal for their metabolic requirements. In E. coli energy taxis encompasses aerotaxis (response to an oxygen gradient) and redox taxis (response to a redox gradient). The molecular mechanisms of energy taxis are closely related to those of chemotaxis whereby bacteria respond to specific chemical attractants and repellents in their external environment (see chemotactic two-component signal transduction).
Energy taxis in E. coli is achieved by a signal transduction system that responds to changes in the electron transport system. Two receptors sense changes in the ET system: Aer and Tsr. Aer senses changes in the redox state of the system via an FAD cofactor while Tsr senses changes in proton motive force that result from perturbation of the ET system. Signals from Aer and Tsr are transduced via the CheA, CheW and CheY proteins, to the flagellar apparatus. CheY influences flagella rotation by direct binding to the FliM protein - a component of the flagella motor switch complex. CheY and phosphoCheY bind to FliM with different affinities, influencing the direction of flagellar rotation and facilitating movement.
Rebbapragada97: Rebbapragada A, Johnson MS, Harding GP, Zuccarelli AJ, Fletcher HM, Zhulin IB, Taylor BL (1997). "The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior." Proc Natl Acad Sci U S A 94(20);10541-6. PMID: 9380671
Rowsell95: Rowsell EH, Smith JM, Wolfe A, Taylor BL (1995). "CheA, CheW, and CheY are required for chemotaxis to oxygen and sugars of the phosphotransferase system in Escherichia coli." J Bacteriol 177(20);6011-4. PMID: 7592359
Barak04: Barak R, Prasad K, Shainskaya A, Wolfe AJ, Eisenbach M (2004). "Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli." J Mol Biol 342(2);383-401. PMID: 15327942
Barak92: Barak R, Welch M, Yanovsky A, Oosawa K, Eisenbach M (1992). "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch." Biochemistry 31(41);10099-107. PMID: 1390767
Bhatnagar12: Bhatnagar J, Sircar R, Borbat PP, Freed JH, Crane BR (2012). "Self-association of the histidine kinase CheA as studied by pulsed dipolar ESR spectroscopy." Biophys J 102(9);2192-201. PMID: 22824284
Borkovich89: Borkovich KA, Kaplan N, Hess JF, Simon MI (1989). "Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer." Proc Natl Acad Sci U S A 86(4);1208-12. PMID: 2645576
Bourret93: Bourret RB, Davagnino J, Simon MI (1993). "The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW." J Bacteriol 175(7);2097-101. PMID: 8384620
Briegel13: Briegel A, Ames P, Gumbart JC, Oikonomou CM, Parkinson JS, Jensen GJ (2013). "The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state." Mol Microbiol 89(5);831-41. PMID: 23802570
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Filimonov93: Filimonov VV, Prieto J, Martinez JC, Bruix M, Mateo PL, Serrano L (1993). "Thermodynamic analysis of the chemotactic protein from Escherichia coli, CheY." Biochemistry 1993;32(47);12906-21. PMID: 8251514
Francis04: Francis NR, Wolanin PM, Stock JB, Derosier DJ, Thomas DR (2004). "Three-dimensional structure and organization of a receptor/signaling complex." Proc Natl Acad Sci U S A 101(50);17480-5. PMID: 15572451
Garzon96: Garzon A, Parkinson JS (1996). "Chemotactic signaling by the P1 phosphorylation domain liberated from the CheA histidine kinase of Escherichia coli." J Bacteriol 178(23);6752-8. PMID: 8955292
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