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Genetics of ribosomal protein methylation in Escherichia coli

II. A mutant lacking a new type of methylated amino acid, N5-methylglutamine, in protein L3

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Summary

The ribosomes of an Escherichia coli mutant, designated prm-2, can be methylated in vitro by an enzymatic fraction from wild-type. This enzyme is inactive on the ribosomes from another mutant, prm-1, reported previously to be methyl group-defidient in protein L11.

In vitro methylation of prm-2 ribosomes resulted in the incorporation of about one methyl group per molecule of protein L3. After acid hydrolysis, all the methyl groups were found in a very basic compound which was identified as methylamine. This compound could have been generated by acid hydrolysis of N-methylated amide-groups from glutamine or asparagine. Therefore, chemically-synthesized N4-methyl-asparagine and N5-methylglutamine were chromatographed together with an enzymatic hydrolysate of methylated prm-2 proteins. In all the chromatographic systems studied the methylated amino acid was found in the same position as N5-methylglutamine. These results indicated that mutant prm-2 lacks one residue of N5-methylglutamine present in ribosomal protein L3 of wild type E. coli.

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Authors and Affiliations

  1. Unité de Cytogénétique, Université de Louvain, Place Croix du Sud 4, B-1348, Louvain-la-Neuve, Belgium

    Jacques Lhoest & Charles Colson

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  1. Jacques Lhoest
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  2. Charles Colson
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Communicated by F. Gros

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Lhoest, J., Colson, C. Genetics of ribosomal protein methylation in Escherichia coli . Molec. Gen. Genet. 154, 175–180 (1977). https://doi.org/10.1007/BF00330833

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  • DOI: https://doi.org/10.1007/BF00330833

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