ISSN:
1617-4623
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00330833
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