Transcript-specific translational regulation in the unfolded protein response of Saccharomyces cerevisiae.
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.
Payne
Tom
T
School of Biology, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Hanfrey
Colin
C
Bishop
Amy L
AL
Michael
Anthony J
AJ
Avery
Simon V
SV
Archer
David B
DB
D001483:Base Sequence; D017931:DNA Primers; D020411:Oligonucleotide Array Sequence Analysis; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
D017931:DNA Primers; D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins