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• W2051245203 abstract "Macrolide antibiotics block the entrance of nascent peptides to the peptide exit tunnel of the large ribosomal subunit. Expression of specific cis-acting peptides confers low-level macrolide-resistance. We show that, in the case of josamycin, peptide expression does not eject josamycin from the ribosome, implying a peptide resistance mechanism different from that previously suggested for erythromycin. We find dipeptide formation and dipeptidyl-tRNA drop-off in the presence of josamycin to be much slower during translation of resistance than of control mRNAs. We demonstrate low-level josamycin resistance by over-expression of peptidyl-tRNA hydrolase. These findings suggest dual growth-inhibitory action of josamycin by (i) direct inhibition of peptide-elongation and (ii) indirect inhibition of peptide-elongation through rapid peptidyl-tRNA drop-off, leading to depletion of tRNA isoacceptors available for protein synthesis. We propose that josamycin resistance peptide expression brings ribosomes into a quarantine state with small drop-off rate, thereby eliminating the josamycin dependent depletion of tRNA isoacceptors in the protein-synthesis-active state." @default.
• W2051245203 created "2016-06-24" @default.
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• W2051245203 date "2009-08-01" @default.
• W2051245203 modified "2023-09-24" @default.
• W2051245203 title "Cis-acting resistance peptides reveal dual ribosome inhibitory action of the macrolide josamycin" @default.
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• W2051245203 doi "https://doi.org/10.1016/j.biochi.2009.05.002" @default.
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