Abstract
STARVATION of an Escherichia coli rel− (RCrel) strain for an essential amino acid results in the synthesis of ribosomal RNA (rRNA) without the concomitant synthesis of proteins1,2. Ribosomal precursor particles accumulate in these conditions and such precursor particles have been shown to be deficient in the methylation of rRNA (ref. 3). We have observed that in addition to proteins L7 and L12, which were previously reported to be methylated4, several other ribosomal proteins from the 50S subunit were also methylated in the unstarved culture5,6. Similar observations have also been made by Alix and Hayes7, but are the precursor particles generated by rel− strain after starvation for methionine also deficient in the methylation of the ribosomal proteins and if so, can such particles be methylated in vitro?
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CHANG, C., CHANG, F. Methylation of ribosomal proteins in vitro. Nature 251, 731–733 (1974). https://doi.org/10.1038/251731a0
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DOI: https://doi.org/10.1038/251731a0
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