Alteration of ribosomal protein L5 in a thiopeptin-resistant mutant of escherichia coli

Streptomycin‐ and viomycin‐induced conformational changes of ribosomes detected by iodination

“…However, it is suggestive that viomycin modifies the labelling of proteins Ll and L5. Protein LS is close to the interaction site of elongation factor (EF) G [25] and is modified in mutants resistant to thiopeptin [26] (an antibiotic that prevents interaction of EF-G and aminoacyl-tRNA with the ribosome [1,2] and there are indications (A. Zamir, 24 personal communication) that protein Ll reacts with a derivative of erythromycin (an antibiotic that under some conditions inhibits translocation [27]). Thus, it is also possible that the alteration of these proteins, or of nearby ribosomal components, may account for the inhibition of translocation by viomycin.…”