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      Functional interaction between tRNA2Gly2 at the ribosomal P-site and RF1 during termination at UAG.

      Journal of Molecular Biology
      Codon, Terminator, genetics, DNA Transposable Elements, Escherichia coli, Escherichia coli Proteins, Glycine, Mutation, Peptide Termination Factors, metabolism, Protein Biosynthesis, RNA, Transfer, Gly, Ribosomes

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          Abstract

          The glycine codons GGA or GGG, on the 5' side of stop codons UAG and UGA, are associated with a uniquely low termination efficiency in Escherichia coli, as compared to other codons, including the two glycine codons GGU and GGC. In contrast to the wild-type strain, all four glycine codons have a similar effect on termination at UAG in a strain with a mutant release factor 1 (RF1). Thus, these two glycine codon pairs, when present at the ribosomal P-site, affect termination efficiency of mutant or wild-type RF1 at UAG differently. If reading of GGA/G by tRNAGly2 is eliminated in the RF1 wild-type strain and replaced by a mutant form of tRNAGly3, termination efficiency is increased to the same level as for GGU/C, normally read by tRNAGly3. The results suggest an unusual interaction between the P-site tRNAGly2 and wild-type RF1 at the ribosomal A-site that is not present with mutant RF1. Copyright 1998 Academic Press

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