17-11)
112,118,119 Although tetracycline is widely used in the clinic, drug resistance due to mutations within the ribosomal binding sites limits its clinical efficacy Antibiotics that directly interfere with peptide bond formation generally do so by preventing the accurate placement of the aminoacylated-CCA-end of the A-tRNA at the PTC (Fig
In our experiments with the EF‐Tu‐promoted system, where translocation was the rate‐limiting step Which antibiotic inhibits interaction between tRNA and mRNA during bacterial protein synthesis? Inhibits binding of aminoacyl tRNA to ribosome: B: Erythromycin: q: Inhibits interaction between tRNA and mRNA: C: Tetracyclines, including doxycycline, prevent the binding of aminoacyl-tRNA by blocking the A (aminoacyl) site of the 30S ribosome
Fusidic acid is a steroidal antibiotic that slows the ribosome at the posttranslocation step
Tetracyclines blocks the A site on the ribosome and prevents the binding of aminoacyl-tRNAs
If CYP3A4 substrates, such as simvastatin (Zocor), lovastatin (Mevacor), or atorvastatin (Lipitor), are taken concomitantly with erythromycin Abstract
Streptomycin interferes with the initial steps of protein synthesis by changing the shape of 30S proton of 70S prokaryotic ribosome
Erythromycin acts by inhibiting the aminoacyl translocation along the ribosomes
Lot and Batch Numbers can be found on The result is that either aminoacyl-tRNA binding or translocation, respectively, pass via the non-enzymatic (factor-free) pathways (Gavrilova et al
We report the first small molecule, KKL-55, that specifically inhibits EF-Tu activity in trans -translation without affecting its activity in normal translation