Methylation, Demethylation, and Deamidation at Glutamate Residues in Membrane Chemoreceptor Proteins

  • Jeff Stock
  • Simon Simms
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)


In bacteria, Chemotaxis toward attractants and away from repellents is mediated by a simple sensing system (for a recent review see Stock, 1987). Stimulatory ligands are detected through their interactions with specific receptors at the cell surface. Information from these peripheral chemoreceptor proteins is transduced into a signal that controls the activity of the flagellar motor so that cells move toward favorable environmental conditions. Six cytoplasmic proteins, the Che proteins, function in conjunction with the transmembrane chemoreceptors to control motility. These have been defined both biochemically and genetically. The corresponding che genes are located in two adjacent operons called Mocha and Meche:
Two of the six proteins are enzymes that catalyze the reversible methylation of receptor glutamate residues. CheR transfers methyl groups from S-adenosylmethionine to these glutamate side chains, and CheB mediates the hydrolysis of the γ-carboxyl methylesters that are produced. This review will focus on the chemistry and enzymology of these and related receptor modification reactions.


Glutamate Residue Bacterial Chemotaxis Stimulatory Ligand Amino Terminal Domain Aspartate Receptor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Jeff Stock
    • 1
  • Simon Simms
    • 1
  1. 1.Department of Molecular BiologyPrinceton UniversityPrincetonUSA

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