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Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition

Abstract : Eukaryote ribosomal translation is terminated when release factor eRF1, in a complex with eRF3, binds to one of the three stop codons. The tertiary structure and dimensions of eRF1 are similar to that of a tRNA, supporting the hypothesis that release factors may act as molecular mimics of tRNAs. To identify the yeast eRF1 stop codon recognition domain (analogous to a tRNA anticodon), a genetic screen was performed to select for mutants with disabled recognition of only one of the three stop codons. Nine out of ten mutations isolated map to conserved residues within the eRF1 N-terminal domain 1. A subset of these mutants, although wild-type for ribosome and eRF3 interaction, differ in their respective abilities to recognize each of the three stop codons, indicating codon-specific discrimination defects. Five of six of these stop codon-specific mutants define yeast domain 1 residues (I32, M48, V68, L123, and H129) that locate at three pockets on the eRF1 domain 1 molecular surface into which a stop codon can be modeled. The genetic screen results and the mutant phenotypes are therefore consistent with a role for domain 1 in stop codon recognition; the topology of this eRF1 domain, together with eRF1-stop codon complex modeling further supports the proposal that this domain may represent the site of stop codon binding itself.
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Contributor : David Ritchie Connect in order to contact the contributor
Submitted on : Saturday, November 21, 2009 - 5:06:49 PM
Last modification on : Wednesday, August 19, 2020 - 10:32:03 AM

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G. Bertram, H.A. Bell, David Ritchie, G. Fullerton, Ian Stansfield. Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition. RNA, Cold Spring Harbor Laboratory Press, 2000, 6 (9), pp.1236-1247. ⟨10.1017/S1355838200000777⟩. ⟨inria-00434274⟩



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