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

• Published in: FEBS letters Vol. 582; no. 4; pp. 503 - 509
• Main Authors: Payne, Tom, Hanfrey, Colin, Bishop, Amy L., Michael, Anthony J., Avery, Simon V., Archer, David B.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 20.02.2008
• Subjects: Base Sequence; DNA Primers; Microarray; Oligonucleotide Array Sequence Analysis; Polysome; Protein Biosynthesis; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger - genetics; Saccharomyces; Saccharomyces cerevisiae; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Stress; Transcription, Genetic; Translation; Unfolded protein response; UPR; Translation; UPR; Saccharomyces; Microarray; Polysome; Stress; Unfolded protein response
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2008.01.009

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.