The Binding of Purified Phe‐tRNA and Peptidyl‐tRNAPhe to Escherichia coli Ribosomes

Nathan DE Groot*, Amos Panet, Yehuda Lapidot

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

The binding of purified Gly3‐Phe‐tRNA to Escherichia coli ribosomes was compared to that of crude Gly3‐Phe‐tRNA (containing bulk tRNA). Gly3‐phe‐tRNA from the purifed preparation binds preferentially to the P site (peptidyl site) at both a high (30 mM) and a low (10 mM) magnesium acetate concentration, while peptidyl‐tRNA from the crude preparation bound more to A site (aminoacyl site) than to the P site at 30 mM magnesium acetate under the same experimental conditions. The addition of tRNAPhe to the purified Gly3‐Phe‐tRNA preparation strongly inhibited the binding at 10mM. At 30 mM Mg2+ the addition of the same amount of tRNAPhe caused the Gly3‐Phe‐tRNA to bind partially to the A site, but did not inhibit the total amount of Gly3‐Phe‐tRNA which binds to the ribosomes. The binding of purified Phe‐tRNA in the presence of T factor and GTP is not inhibited by tetracycline. However, tetracycline strongly inhibited the enzymatic binding of Phe‐tRNA when tRNAPhe was added. From the results presented in this paper it is proposed that in the presence of poly(U), Phe‐tRNA or peptidyl‐tRNAPhe can bind to A sites only of those ribosomes which have their P site occupied by tRNA or one of its derivatives (aminoacyl‐tRNA or peptidyl‐tRNA).

Original languageEnglish
Pages (from-to)523-527
Number of pages5
JournalEuropean Journal of Biochemistry
Volume23
Issue number3
DOIs
StatePublished - Dec 1971

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