Characterization of methylated neutral amino acids from Escherichia coli ribosomes

J Bacteriol. 1977 Jul;131(1):105-10. doi: 10.1128/jb.131.1.105-110.1977.

Abstract

The methylated neutral amino acids from both 30S and 50S ribosomal subunits of an Escherichia coli K strain were characterized. The 50S ribosomal subunit contains three methylated neutral amino acids: N-monomethylalanine, N-monomethylmethionine, and an as yet unidentified methylated amino acid found in protein L11. Both N-monomethylalanine and N-monomethylmethionine were found in protein L33. The amount of N-monomethylmethionine in this protein, however, is variable but not more than 0.25 molecules per protein. Thus protein L33 from this E. coli K strain has heterogeneity in its N-terminal amino acid and can start with either N-monomethylalanine or N-monomethylmethionine. The N-monomethylmethionine residue was not derived from the reduction of N-formylmethionine in the protein. The 30S ribosomal subunit contains only one methylated neutral amino acid: N-monomethylalanine.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alanine / analogs & derivatives*
  • Alanine / analysis
  • Bacterial Proteins / analysis*
  • Escherichia coli / analysis*
  • Escherichia coli / metabolism
  • Methionine / analogs & derivatives*
  • Methionine / analysis
  • Methylation
  • N-Formylmethionine / metabolism
  • Ribosomal Proteins / analysis*

Substances

  • Bacterial Proteins
  • Ribosomal Proteins
  • N-Formylmethionine
  • Methionine
  • Alanine