Genetics of ribosomal protein methylation in Escherichia coli. I. A mutant deficient in methylation of protein L11.
Several thousand mutagenized clones of Escherichia coli were screened for methyl group incorporation into protein in crude extracts, in order to isolate mutants lacking the full complement of methyl groups in ribosomal proteins. One mutant isolated by this method and designated prm-1 incorporated 6-7 methyl groups per ribosome upon incubation of its ribosomes with a partially purified enzyme preparation from E. coli wild-type. The methyl groups were located exclusively in the 50S particle and for the most part (85%) in protein L11. Three methylated amino acids were detected: epsilon-N-trimethyllysine, epsilon-N-monomethyllysine, and an uncharacterized amino acid. These accounted respectively for 4.6, 1.3 and 0.9 methyl groups per ribosome. These results indicate that protein L11 in wild-type contains a stoichiometric amount of these methylated amino acids which are absent in mutant prm-1. Since this mutant is fully viable, its methylation deficiency does not result in a major defect in ribosome assembly or functioning.
D000596:Amino Acids / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D066298:In Vitro Techniques; D008239:Lysine / Q000031:analogs & derivatives / Q000302:isolation & purification; D008745:Methylation; D009154:Mutation; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism
D000596:Amino Acids; D001426:Bacterial Proteins; D012269:Ribosomal Proteins; D008239:Lysine