N-terminal extension of Saccharomyces cerevisiae translation termination factor eRF3 influences the suppression efficiency of sup35 mutations

FEMS Yeast Res. 2007 May;7(3):357-65. doi: 10.1111/j.1567-1364.2006.00176.x. Epub 2007 Feb 16.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alleles
  • Blotting, Western
  • Gene Expression Regulation, Fungal / genetics*
  • Models, Molecular
  • Mutagenesis, Insertional
  • Peptide Termination Factors / biosynthesis
  • Peptide Termination Factors / genetics*
  • Peptide Termination Factors / metabolism
  • Plasmids / genetics
  • Prions / genetics*
  • Protein Biosynthesis*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / biosynthesis
  • Saccharomyces cerevisiae Proteins / genetics*

Substances

  • Peptide Termination Factors
  • Prions
  • SUP35 protein, S cerevisiae
  • SUP45 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins