The effect of GTP hydrolysis and transpeptidation on the arrangement of aminoacyl‐tRNA at the A‐site of Escherichia coli 70 S ribosomes
- 25 February 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 181 (2) , 367-372
- https://doi.org/10.1016/0014-5793(85)80294-5
Abstract
From 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.Keywords
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