Regulation of chemotaxis in bacteria
Environmental signals are detected by the chemotactic receptors, located in the cytoplasmic membrane, and transduced via several proteins to the flagella which eventually affect the movement of the cell. The receptor can be reversibly methylated and induces reversible phosphorylation of a cytoplasmic protein, CheA, which appears to be the major regulatory site in chemotaxis. Recently, we have found that CheA can also be methylated and we are trying to evaluate the importance of this methylation in signal transduction.
Subbaramaiah, K., and Simms, S.A. (1992) Photolabeling of CheR Methyltransferase with S-Adenosyl-L-Methionine: Studies on the AdoMet Binding Site. J. Biol. Chem. 267, 8636-8642.
Simms, S.A., and Subbaramaiah, K. (1991) The Kinetic Mechanism of S-Adenosyl-L-methionine: Glutamyl methyltransferase from Salmonella tryphimurium. J. Biol. Chem. 266, 12741-12746.
Subbaramiah, K., Charles, H., and Simms, S.A. (1991) Probing the Role of Cysteine Residues in the CheR Methyltransferase. J. Biol. Chem. 266, 19023-19027.