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• W1978966052 abstract "In eukaryotic ribosomes, termination of translation is triggered by class 1 polypeptide release factor, eRF1. In organisms with a universal code, eRF1 responds to three stop codons, whereas, in ciliates with variant codes, only one or two codon(s) remain(s) as stop signals. By mutagenesis of the Y-C-F minidomain of the N domain, we converted an omnipotent human eRF1 recognizing all three stop codons into a unipotent 'ciliate-like' UGA-only eRF1. The conserved Cys127 located in the Y-C-F minidomain plays a critical role in stop codon recognition. The UGA-only response has also been achieved by concomitant substitutions of four other amino acids located at the Y-C-F and NIKS minidomains of eRF1. We suggest that for eRF1 the stop codon decoding is of a non-linear (non-protein-anticodon) type and explores a combination of positive and negative determinants. We assume that stop codon recognition is profoundly different by eukaryotic and prokaryotic class 1 RFs." @default.
• W1978966052 created "2016-06-24" @default.
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• W1978966052 date "2002-09-01" @default.
• W1978966052 modified "2023-10-17" @default.
• W1978966052 title "Conversion of omnipotent translation termination factor eRF1 into ciliate‐like UGA‐only unipotent eRF1" @default.
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• W1978966052 doi "https://doi.org/10.1093/embo-reports/kvf178" @default.
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