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Nucleic Acids Research, 1977, Vol. 4, No. 7 2205-2212
© 1977

Articles

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* and Friedrich Cramer*

Department of Biological Chemistry, The Hebrew University of Jerusalem Israel *Abteilung Chemie, Max-Planck-Institut für experimentelle Medizin D-34 Göttingen, Hermann-Rein-Str. 3, GFR

Received March 30, 1977. 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.


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