The effect of GTP hydrolysis and transpeptidation on the arrangement of aminoacyl-tRNA at the A-site of Escherichia coli 70 S ribosomes

AbstractFrom the affinity labelling of 70 S ribosomes with a photoreactive derivative of Phe-tRNAphe bearing an arylazido group on guanine residues, it has been found that different sets of ribosomal proteins are labelled in the course of three successive steps of EF-Tu-dependent binding of aminoacyl-tRNA derivative at the A-site. Proteins S5, S7, S8, S16, S17, L9, L14, L15 and L24 were labelled before GTP hydrolysis; proteins S5, S7, S9, S11, S14, S18, S19, S21, L9, L21 and L29 - after GTP hydrolysis; proteins S2, S5, S7, S21, L11 and L23 - after GTP hydrolysis and transpeptidation