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Methylation of Ribosomal Proteins in Escherichia coli

¹ Department of Biology, Temple University, Philadelphia, Pennsylvania 19122, and Fels Research Institute and Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140

ABSTRACT

Escherichia coli was grown in a medium containing [1-¹⁴C]methionine and [methyl-³H]methionine, and the ³H/¹⁴C 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 -trimethyllysine. A small amount of a compound tentatively identified as N^G, N'^G-dimethylarginine was also detected.