Transcript-specific translational regulation in the unfolded protein response of Saccharomyces cerevisiae

Tom Payne, Colin Hanfrey, Amy L. Bishop, Anthony J. Michael, Simon V. Avery, David B. Archer

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


Accumulation of unfolded proteins in the endoplasmic reticulum (ER) causes stress and induces the unfolded protein response (UPR). Genome-wide analysis of translational regulation in response to the UPR-inducing agent dithiothreitol in Saccharomyces cerevisiae is reported. Microarray analysis, confirmed using qRT-PCR, identified transcript-specific translational regulation. Transcripts with functions in ribosomal biogenesis and assembly were translationally repressed. In contrast, mRNAs from known UPR genes, encoding the UPR transcription factor Hac1p, the ER-oxidoreductase Ero1p and the ER-associated protein degradation (ERAD) protein Der1p, were enriched in polysomal fractions, indicating translational up-regulation. Splicing of HAC1 mRNA is shown to be required for efficient ribosomal loading.

Original languageEnglish (US)
Pages (from-to)503-509
Number of pages7
JournalFEBS Letters
Issue number4
StatePublished - Feb 20 2008


  • Microarray
  • Polysome
  • Saccharomyces
  • Stress
  • Translation
  • UPR
  • Unfolded protein response

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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