TY - JOUR
T1 - Properties of phenylalanine transfer ribonucleic acid with modified 3′-terminal end in protein biosynthesis using a rabbit reticulocyte cell-free system
T2 - Effect of the replacement of cytidine residues from the CpCpA end of tRNA by 5-iodocytidine or 2-thiocytidine
AU - Keshet (baksht), Eli
AU - Gal, Alma
AU - Groot, Nathan De
AU - Hochberg, Abraham A.
AU - Sprinzl, Mathias
AU - Cramer, Friedrich
PY - 1977/7
Y1 - 1977/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0017372893&partnerID=8YFLogxK
U2 - 10.1093/nar/4.7.2205
DO - 10.1093/nar/4.7.2205
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C2 - 242797
AN - SCOPUS:0017372893
SN - 0305-1048
VL - 4
SP - 2205
EP - 2212
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 7
ER -