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. 1974 Nov;120(2):651–656. doi: 10.1128/jb.120.2.651-656.1974

Methylation of Ribosomal Proteins in Escherichia coli

F N Chang 1, C N Chang 1, Woon Ki Paik 1
PMCID: PMC245823  PMID: 4616944

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 ε-trimethyllysine. A small amount of a compound tentatively identified as NG, N′G-dimethylarginine was also detected.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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