PMID:3298225

Citation	Stock, A, Schaeffer, E, Koshland, DE Jr and Stock, J (1987) A second type of protein methylation reaction in bacterial chemotaxis. J. Biol. Chem. 262:8011-4
Abstract	CheZ is the product of one of six genes required for sensory processing in Escherichia coli and Salmonella typhimurium chemotaxis. This 24-kDa cytoplasmic protein is modified by a posttranslational methylation reaction. The modified residue has been identified by analysis of radioactively labeled protein from two-dimensional electrophoretograms and Edman degradation of CheZ protein isolated by immunoaffinity chromatography using anti-CheZ monoclonal antibodies. The methylated group is an N-monomethylmethionine residue at the amino terminus of CheZ. L16, a ribosomal protein that is required for peptidyltransferase activity during protein synthesis, is also methylated at its amino-terminal methionine (Chen, R., Brosius, J., and Wittmann-Liebold, B. (1977) J. Mol. Biol. 111, 173-181). Homologous sequences at the amino termini of L16 and CheZ raise the possibility that a single S-adenosylmethionine-dependent methyltransferase modifies both proteins.
Links	PubMed
Keywords	Bacterial Proteins; Chemotactic Factors/metabolism; Chemotaxis; Genes; Genes, Bacterial; Membrane Proteins/genetics; Membrane Proteins/isolation & purification; Membrane Proteins/metabolism; Methylation; Salmonella typhimurium/genetics; Salmonella typhimurium/physiology
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