title: Methylation of ribosomal proteins in Escherichia coli.
abstract: Escherichia coli was grown in a medium containing [1-(14)C]methionine and [methyl-(3)H]methionine, and the (3)H/(14)C ratio was determined for each of the ribosomal proteins derived from the 70S ribosome. Evidence indicates that six proteins from the 50S subunit were methylated: L7, L9, L11, L12, L18, and L33. Methylation of several other 50S proteins (such as L1, L3, L5, etc.) may also occur. The methylated amino acids in protein L11 have been characterized further and found to be predominately epsilon-trimethyllysine. A small amount of a compound tentatively identified as N(G), N'(G)-dimethylarginine was also detected.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001322:Autoanalysis; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002250:Carbon Radioisotopes; D003470:Culture Media; D004590:Electrophoresis, Paper; D004926:Escherichia coli / Q000378:metabolism*; D008239:Lysine / Q000031:analogs & derivatives / Q000032:analysis; D008715:Methionine / Q000378:metabolism; D008745:Methylation; D012270:Ribosomes / Q000378:metabolism*; D014316:Tritium
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D003470:Culture Media; D014316:Tritium; D008715:Methionine; D008239:Lysine