The effect of GTP hydrolysis and transpeptidation on the arrangement of aminoacyl-tRNA at the A-site of Escherichia coli 70 S ribosomes |
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| Authors: | R A Gabbay |
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| Affiliation: | 1. Institute of Bioorganic Chemistry, Siberian Division of the USSR Academy of Sciences, Novosibirsk, 630090 USSR;2. B.P. Konstantinov Nuclear Physics Institute of the USSR Academy of Sciences, Gatchina, Leningrad District 188350, USSR |
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| 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. |
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