Role of the constant uridine in binding of yeast tRNAPhe anticodon arm to 30S ribosomes. Journal Article uri icon



  • Twenty-two anticodon arm analogues were prepared by joining different tetra, penta, and hexaribonucleotides to a nine nucleotide fragment of yeast tRNAPhe with T4 RNA ligase. The oligomer with the same sequence as the anticodon arm of tRNAPhe bind poly U programmed 30S ribosomes with affinity similar to intact tRNAPhe. Analogues with an additional nucleotide in the loop bind ribosomes with a weaker affinity whereas analogues with one less nucleotide in the loop do not bind ribosomes at all. Reasonably tight binding of anticodon arms with different nucleotides on the 5' side of the anticodon suggest that positions 32 and 33 in the tRNAPhe sequence are not essential for ribosome binding. However, differences in the binding constants for anticodon arms containing modified uridine residues in the "constant uridine" position suggest that both of the internal "U turn" hydrogen bonds predicted by the X-ray crystal structure are necessary for maximal ribosome binding.

publication date

  • June 11, 1982

has subject area

has restriction

  • green

Date in CU Experts

  • March 13, 2015 12:57 PM

Full Author List

  • Uhlenbeck OC; Lowary PT; Wittenberg WL

author count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 0305-1048

Additional Document Info

start page

  • 3341

end page

  • 3352


  • 10


  • 11