Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding. Journal Article uri icon



  • To better understand why aminoacyl-tRNAs (aa-tRNAs) have evolved to bind bacterial elongation factor Tu (EF-Tu) with uniform affinities, mutant tRNAs with differing affinities for EF-Tu were assayed for decoding on Escherichia coli ribosomes. At saturating EF-Tu concentrations, weaker-binding aa-tRNAs decode their cognate codons similarly to wild-type tRNAs. However, tighter-binding aa-tRNAs show reduced rates of peptide bond formation due to slow release from EF-Tu•GDP. Thus, the affinities of aa-tRNAs for EF-Tu are constrained to be uniform by their need to bind tightly enough to form the ternary complex but weakly enough to release from EF-Tu during decoding. Consistent with available crystal structures, the identity of the esterified amino acid and three base pairs in the T stem of tRNA combine to define the affinity of each aa-tRNA for EF-Tu, both off and on the ribosome.

publication date

  • March 29, 2011

has subject area

has restriction

  • green

Date in CU Experts

  • March 13, 2015 12:56 PM

Full Author List

  • Schrader JM; Chapman SJ; Uhlenbeck OC

author count

  • 3

Other Profiles

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

Additional Document Info

start page

  • 5215

end page

  • 5220


  • 108


  • 13