The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid. Journal Article uri icon

Overview

abstract

  • When different mutations were introduced into the anticodon loop and at position 73 of YFA2, a derivative of yeast tRNA(Phe), 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.

publication date

  • May 1, 2004

has subject area

Date in CU Experts

  • March 13, 2015 12:56 PM

Full Author List

  • Dale T; Sanderson LE; Uhlenbeck OC

author count

  • 3

citation count

  • 27

Other Profiles

International Standard Serial Number (ISSN)

  • 0006-2960

Electronic International Standard Serial Number (EISSN)

  • 1520-4995

Additional Document Info

start page

  • 6159

end page

  • 6166

volume

  • 43

issue

  • 20