N-terminal extension of Saccharomyces cerevisiae translation termination factor eRF3 influences the suppression efficiency of sup35 mutations.
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.
Volkov
Kirill
K
Department of Genetics, St Petersburg State University, St Petersburg, Russia.
Osipov
Kirill
K
Valouev
Igor
I
Inge-Vechtomov
Sergey
S
Mironova
Ludmila
L
D000483:Alleles; D015153:Blotting, Western; D015966:Gene Expression Regulation, Fungal / Q000235:genetics*; D008958:Models, Molecular; D016254:Mutagenesis, Insertional; D010454:Peptide Termination Factors / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D010957:Plasmids / Q000235:genetics; D011328:Prions / Q000235:genetics*; D014176:Protein Biosynthesis; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis / Q000235:genetics*
D010454:Peptide Termination Factors; D011328:Prions; C068068:SUP35 protein, S cerevisiae; C080775:SUP45 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins