The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid

Taraka Dale, Lee E. Sanderson, Olke C. Uhlenbeck*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

77 Scopus citations

Abstract

When different mutations were introduced into the anticodon loop and at position 73 of YFA2, a derivative of yeast tRNAPhe, a single tRNA body was misacylated with 13 different amino acids. The affinities of these misacylated tRNAs for Thermus thermophilus elongation factor Tu (EF-Tu)·GTP were determined using a ribonuclease protection assay. A range of 2.5 kcal/mol in the binding energies was observed, clearly demonstrating that EF-Tu specifically recognizes the side chain of the esterified amino acid. Furthermore, this specificity can be altered by introducing a mutation in the amino acid binding pocket on the surface of EF-Tu. Also, when discussed in conjunction with the previously determined specificity of EF-Tu for the tRNA body, these experiments further demonstrate that EF-Tu uses thermodynamic compensation to bind cognate aminoacyl-tRNAs similarly.

Original languageEnglish (US)
Pages (from-to)6159-6166
Number of pages8
JournalBiochemistry
Volume43
Issue number20
DOIs
StatePublished - May 25 2004

ASJC Scopus subject areas

  • Biochemistry

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