In vivo methylation of elongation factor Tu of Escherichia coli.
A protein existing mainly in the supernatant fraction of Escherichia coli was found to be methylated by accepting the methyl moiety originating from methionine. The protein was identified as peptide synthesis elongation factor Tu (EF-Tu) by the following criteria. 1) The methylatable protein separated at the same position as purified EF-Tu on two-dimensional gel electrophoresis. 2) The methylatable protein interacted with antiserum specific for EF-Tu. Amino acid analysis of the methyl-labeled protein suggested that the site of methylation was an epsilon-amino group of lysine.
D000596:Amino Acids / Q000032:analysis; D004926:Escherichia coli / Q000378:metabolism*; D005779:Immunodiffusion; D007700:Kinetics; D008239:Lysine / Q000032:analysis; D008715:Methionine; D008745:Methylation; D008970:Molecular Weight; D010445:Peptide Elongation Factors / Q000378:metabolism*
D000596:Amino Acids; D010445:Peptide Elongation Factors; D008715:Methionine; D008239:Lysine