Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination
| Autor: | Ming Du, Joe Salas-Marco, Kim M. Keeling, David M. Bedwell, Andrey V. Pisarev, Sunnie R. Thompson, Tatyana V. Pestova, Hua Fan-Minogue, Adam K. Kallmeyer |
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| Rok vydání: | 2008 |
| Předmět: |
Protein Conformation
Recombinant Fusion Proteins Saccharomyces cerevisiae Amino Acid Motifs Euplotes Peptide Models Biological Article Eukaryotic translation Suppression Genetic Animals Euplotes octocarinatus Molecular Biology chemistry.chemical_classification Genetics biology Cell Biology Peptide Chain Termination Translational biology.organism_classification Genetic code Stop codon Open reading frame chemistry Codon Terminator Peptides Amber Stop Codon Peptide Termination Factors |
| Zdroj: | Molecular cell. 30(5) |
| ISSN: | 1097-4164 |
| Popis: | Organisms that use the standard genetic code recognize UAA, UAG, and UGA as stop codons, whereas variant code species frequently alter this pattern of stop codon recognition. We previously demonstrated that a hybrid eRF1 carrying the Euplotes octocarinatus domain 1 fused to Saccharomyces cerevisiae domains 2 and 3 (Eo/Sc eRF1) recognized UAA and UAG, but not UGA, as stop codons. In the current study, we identified mutations in Eo/Sc eRF1 that restore UGA recognition and define distinct roles for the TASNIKS and YxCxxxF motifs in eRF1 function. Mutations in or near the YxCxxxF motif support the cavity model for stop codon recognition by eRF1. Mutations in the TASNIKS motif eliminated the eRF3 requirement for peptide release at UAA and UAG codons, but not UGA codons. These results suggest that the TASNIKS motif and eRF3 function together to trigger eRF1 conformational changes that couple stop codon recognition and peptide release during eukaryotic translation termination. |
| Databáze: | OpenAIRE |
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