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

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Advances in Post-Translational Modifications of Proteins and Aging

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

Abstract

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.

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  1. Department of Molecular Biology, Princeton University, Princeton, N.J., USA

    Ann Stock

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  1. University of Naples, Naples, Italy

    Vincenzo Zappia , Patrizia Galletti  & Raffaele Porta ,  & 

  2. University of Texas Health Science Center, Houston, Texas, USA

    Finn Wold

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Stock, A. (1988). N-Methylmethionine at the Amino Terminus of a Protein Required for Bacterial Chemotaxis. In: Zappia, V., Galletti, P., Porta, R., Wold, F. (eds) Advances in Post-Translational Modifications of Proteins and Aging. Advances in Experimental Medicine and Biology, vol 231. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9042-8_31

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