Journal
FEBS LETTERS
Volume 582, Issue 4, Pages 503-509Publisher
WILEY
DOI: 10.1016/j.febslet.2008.01.009
Keywords
unfolded protein response; UPR; stress; microarray; translation; polysome; Saccharomyces
Funding
- Biotechnology and Biological Sciences Research Council Funding Source: Medline
- NIGMS NIH HHS [R01 GM57945] Funding Source: Medline
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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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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