Uniform binding of aminoacylated transfer RNAs to the ribosomal A and P sites. Journal Article uri icon

Overview

abstract

  • The association and dissociation rate constants of eight different E. coli aminoacyl-tRNAs (aa-tRNAs) for E. coli ribosomes programmed with mRNAs of defined sequences were determined. Identical association and dissociation rate constants were observed for all eight aa-tRNAs in both the ribosomal A and P sites despite substantial differences in tRNA sequence, the type of esterified amino acid, and posttranscriptional modifications. These results indicate that the overall binding of all aa-tRNAs to the ribosome is uniform. However, when either the esterified amino acid or the tRNA modifications were removed, binding was no longer uniform. These results suggest that differences in tRNA sequences and tRNA modifications have evolved to offset differential thermodynamic contributions of the esterified amino acid and the codon-anticodon interaction so that ribosomal binding of all aa-tRNAs remains uniform.

publication date

  • December 1, 2004

has subject area

Date in CU Experts

  • March 13, 2015 12:56 PM

Full Author List

  • Fahlman RP; Dale T; Uhlenbeck OC

author count

  • 3

citation count

  • 42

Other Profiles

International Standard Serial Number (ISSN)

  • 1097-2765

Electronic International Standard Serial Number (EISSN)

  • 1097-4164

Additional Document Info

start page

  • 799

end page

  • 805

volume

  • 16

issue

  • 5