A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity†

@inproceedings{Eliseev2011ASA,
  title={A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity†},
  author={Boris Eliseev and Polina Kryuchkova and Elena Alkalaeva and Ludmila Frolova},
  booktitle={Nucleic Acids Research},
  year={2011}
}
In eukaryotes a single class-1 translation termination factor eRF1 decodes the three stop codons: UAA, UAG and UGA. Some ciliates, like Euplotes, have a variant code, and here eRF1s exhibit UAR-only specificity, whereas UGA is reassigned as a sense codon. Since eukaryote eRF1 stop-codon recognition is associated with its N-terminal domain, structural features should exist in the N domain of ciliate eRF1s that restrict their stop-codon specificity. Using an in vitro reconstituted eukaryotic… CONTINUE READING
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