N-Methylmethionine at the Amino Terminus of a Protein Required for Bacterial Chemotaxis

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


The methylation of glutamate residues during Chemotaxis has been extensively investigated in Escherichia coli and Salmonella typhimurium (see Stock and Simms, this volume). This reaction is thought to function to modulate the activities of receptor proteins located in the cytoplasmic membrane. Levels of glutamate methylation are controlled by the activities of specific enzymes: the CheR methyltransferase adds groups and the CheB methylesterase removes them. Although reversible methylation at glutamates provides an important adaptive function in chemosensing, it is not essential for Chemotaxis, and mutants completely deficient in both the CheR and CheB enzymes retain an ability to migrate towards favorable environmental conditions. Genetic studies indicate that four cytoplasmic proteins are essential for Chemotaxis, CheA, CheW, CheY, and CheZ (Table 1). These appear to provide a link between chemoreceptors in the membrane and the flagellar motor. One of these components, the CheZ protein, is methylated at its amino terminus (Stock et al., 1987c). Both in terms of its function and chemistry, CheZ methylation is quite different from the reversible methylation that occurs at glutamate residues in the receptors.


Myosin Light Chain Methyl Transferase Bacterial Chemotaxis Flagellar Motor Flagellar Rotation 
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© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Ann Stock
    • 1
  1. 1.Department of Molecular BiologyPrinceton UniversityPrincetonUSA

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