Abstract
The eukaryotic translation termination factor eRF3 stimulates release of nascent polypeptides from the ribosome in a GTP-dependent manner. In most eukaryotes studied, eRF3 consists of an essential, conserved C-terminal domain and a nonessential, nonconserved N-terminal extension. However, in some species, this extension is required for efficient termination. Our data show that the N-terminal extension of Saccharomyces cerevisiae eRF3 also participates in regulation of termination efficiency, but acts as a negative factor, increasing nonsense suppression efficiency in sup35 mutants containing amino acid substitutions in the C-terminal domain of the protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alleles
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Blotting, Western
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Gene Expression Regulation, Fungal / genetics*
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Models, Molecular
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Mutagenesis, Insertional
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Peptide Termination Factors / biosynthesis
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Peptide Termination Factors / genetics*
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Peptide Termination Factors / metabolism
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Plasmids / genetics
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Prions / genetics*
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Protein Biosynthesis*
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / biosynthesis
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Saccharomyces cerevisiae Proteins / genetics*
Substances
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Peptide Termination Factors
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Prions
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SUP35 protein, S cerevisiae
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SUP45 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins