Quantitative analysis of deoxynucleotide substitutions in the codon-anticodon helix. Journal Article uri icon



  • The role of 2' hydroxyl groups in the codon-anticodon helix was evaluated by introducing single deoxynucleotides into each of the six positions in the helix and measuring the affinity of tRNA to either the A site or the P site of Escherichia coli 70S ribosomes. In perfect agreement with the X-ray structure of the Thermus thermophilus 30S subunit, A site binding was weaker in five of the six positions but P site binding was unaffected. Since the addition of paromomycin restores A site binding, it appears that the deoxynucleotide substituted complexes are impaired in their ability to promote the ribosomal conformational change that accompanies tRNA binding.

publication date

  • February 3, 2006

has subject area

has restriction

  • closed

Date in CU Experts

  • March 13, 2015 12:56 PM

Full Author List

  • Fahlman RP; Olejniczak M; Uhlenbeck OC

author count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 0022-2836

Additional Document Info

start page

  • 887

end page

  • 892


  • 355


  • 5