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Eukaryotic Polyribosome Profile Analysis
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Ribosome-bound Pub1 modulates stop codon decoding during translation termination in yeast.

Valery N Urakov1, Olga V Mitkevich1, Irina V Safenkova1

  • 1Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Bach Institute of Biochemistry, Moscow, Russia.

The FEBS Journal
|May 4, 2017
PubMed
Summary

Pub1, a yeast protein, fine-tunes translation termination by interacting with release factor eRF3 and associating with heavy polysomes. Its absence impacts nonsense readthrough efficiency, highlighting its role as an accessory translation factor.

Keywords:
Saccharomyces cerevisiaePub1eRF1eRF3ribosometranslation terminationyeast

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Translation termination in eukaryotes involves release factors eRF1 and eRF3, and ABCE1 for ribosome recycling.
  • Pub1 is a yeast protein previously linked to stress granules, gene expression, and cytoskeleton organization.

Purpose of the Study:

  • To investigate the role of the yeast protein Pub1 in translation termination.
  • To elucidate Pub1's interaction with translation termination machinery and its functional impact.

Main Methods:

  • High velocity sedimentation in sucrose gradients to analyze Pub1-ribosome association.
  • Assessing nonsense readthrough efficiency in the absence of Pub1.

Main Results:

  • Pub1 binds to ribosomes independently of eRF1 and eRF3.
  • Pub1 interacts with eRF3's prion domain via its C-terminal tract.
  • Pub1 associates with heavy polysomes, indicating involvement in active translation termination.
  • Loss of Pub1 reduces nonsense readthrough efficiency at most, but not all, stop signals.

Conclusions:

  • Pub1 functions as an accessory translation factor.
  • Pub1 plays a role in the fine-tuning of translation termination, distinct from other release factor partners.
  • Pub1's specific modulation of readthrough suggests a nuanced role in decoding stop signals.