Add time:08/15/2019         Source:sciencedirect.com

The antibiotic thermorubin specifically inhibits protein synthesis when added to growing cultures of Escherichia coli, while RNA and DNA synthesis are not affected. In vitro studies show that thermorubin is a specific inhibitor of initiation of protein synthesis directed by natural mRNA. The drug inhibits protein synthesis directed by MS2 RNA but not poly(U)-dependent polyphenylalanine synthesis. Furthermore, during protein synthesis directed by endogenous messenger RNA, only the fraction of polypeptide synthesis dependent on ex novo-synthesized mRNA is sensitive to the drug. Thermorubin inhibits the binding of fMet—tRNA to ribosomes in the presence of AUG, GTP and initiation factors whereas the synthesis of the first peptide bond, assayed as fMet-puromycin synthesis, is not impaired by the antibiotic. The implications of these findings, with respect to the hypothesis that RNA synthesis in E. coli is controlled by initiation of protein synthesis, are discussed.

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