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Article

How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?

Journal of molecular biology - 20 Feb 1990

Ehrenberg M, Rojas A M, Weiser J, Kurland C G

Abstract excerpt

We have observed that two EF-Tu.GTP cycles are required to make one peptide bond during steady-state translation in an accurate and fast poly(U) translation system prepared from Escherichia coli. We have also found that there are two complexes of EF-Tu.GTP bound to one molecule of aminoacyl-tRNA under our experimental conditions. We suggest, on the basis of these data, that aminoacyl-tRNA enters the ribosomal...

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Source

Identifiers

PMID: 2179565
DOI: 10.1016/0022-2836(90)90074-V

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?PMID 2179565Read ↗

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Mutants of EF-Tu defective in binding aminoacyl-tRNA.Semantic proximity Read ↗

Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots.Semantic proximity Read ↗

A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome.Semantic proximity Read ↗

Two proofreading steps amplify the accuracy of genetic code translation.Semantic proximity Read ↗

Probing the reactivity of the GTP- and GDP-bound conformations of elongation factor Tu in complex with the antibiotic GE2270 A.Semantic proximity Read ↗

Mechanism of activation of elongation factor Tu by ribosome: catalytic histidine activates GTP by protonation.Semantic proximity Read ↗

Mechanism of translation based on intersubunit complementarities of ribosomal RNAs and tRNAs.Semantic proximity Read ↗

Mutation of the conserved Gly94 and Gly126 in elongation factor Tu from Escherichia coli. Elucidation of their structural and functional roles.Semantic proximity Read ↗

Labeled EF-Tus for rapid kinetic studies of pretranslocation complex formation.Semantic proximity Read ↗

Small protein B interacts with the large and the small subunits of a stalled ribosome during trans-translation.Semantic proximity Read ↗

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