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Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation.

Recent studies of translational control suggest that translation termination may not be simply the end of synthesizing a protein but rather be involved in modulating both the translation efficiency and stability of a given transcript. Using recombinant eukaryotic release factor 3 (eRF3) and cellular extracts, we have shown for Saccharomyces cerevisiae that yeast eRF3 and Pab1p can interact. This interaction, mediated by the N+M domain of eRF3 and amino acids 473 to 577 of Pab1p, was demonstrated to be direct by the two-hybrid approach. We confirmed that a genetic interaction exists between eRF3 and Pab1p and showed that Pab1p overexpression enhances the efficiency of termination in SUP35 (eRF3) mutant and [PSI(+)] cells. This effect requires the interaction of Pab1p with eRF3. These data further strengthen the possibility that Pab1p has a role in coupling translation termination events with initiation of translation. Several lines of evidence indicate that Pab1p does not influence [PSI(+)] propagation. First, "[PSI(+)]-no-more" mutations do not affect eRF3-Pab1p two-hybrid interaction. Second, overexpression of PAB1 does not cure the [PSI(+)] phenotype or solubilize detectable amounts of eRF3. Third, prion-curing properties of overexpressed HSP104p, which is required for formation and maintenance of [PSI(+)], were not modified by excess Pab1p.

Pubmed ID: 11971964


  • Cosson B
  • Couturier A
  • Chabelskaya S
  • Kiktev D
  • Inge-Vechtomov S
  • Philippe M
  • Zhouravleva G


Molecular and cellular biology

Publication Data

May 24, 2002

Associated Grants


Mesh Terms

  • Carrier Proteins
  • Cytoskeletal Proteins
  • Fungal Proteins
  • Gene Expression Regulation, Fungal
  • Humans
  • Peptide Termination Factors
  • Poly(A)-Binding Proteins
  • Prions
  • Protein Binding
  • Protein Biosynthesis
  • RNA-Binding Proteins
  • Receptors, Cytoplasmic and Nuclear
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Two-Hybrid System Techniques