Properties of phenylalanine transfer ribonucleic acid with modified 3′-terminal end in protein biosynthesis using a rabbit reticulocyte cell-free system: Effect of the replacement of cytidine residues from the CpCpA end of tRNA by 5-iodocytidine or 2-thiocytidine

Eli Keshet (baksht)*, Alma Gal, Nathan De Groot, Abraham A. Hochberg, Mathias Sprinzl, Friedrich Cramer

*Corresponding author for this work

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4 Scopus citations

Abstract

Phe-tRNAphe from yeast containing 2-thiocytidine or 5-iodocytidine in position 75 of the polynucleotide chain or Phe-tRNAphe in which both positions 74 and 75 were substituted by 5-lodocytidine were investigated in the poly U-dependent polyphenylalanine synthesis on ribosomes from rabbit reticulocytes. Phe-tRNAphe Cps2CpA was nearly as active as the native Phe-tRNAphe-CpCpA in the overall process. Phe-tRNAPhe-Cpi5CpA as well as Phe-tRNAPhe-i5Cpi5CpA were considerably less active than the native species. In vestigation of individual steps of protein biosynthesis with these modified substrates revealed that the donor activity of peptidyl-tRNAs which contain 5-iodocytidine in their 3′-terminus is strongly impaired suggesting exacting structural requirements for the interaction of the CpCpA end of tRNA with the ribosomal P-site.

Original languageEnglish
Pages (from-to)2205-2212
Number of pages8
JournalNucleic Acids Research
Volume4
Issue number7
DOIs
StatePublished - Jul 1977

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