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

doi:10.1016/j.febslet.2008.01.009

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 journal › Article › peer-review

27 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	503-509
Number of pages	7
Journal	FEBS Letters
Volume	582
Issue number	4
DOIs	https://doi.org/10.1016/j.febslet.2008.01.009
State	Published - Feb 20 2008

Keywords

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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10.1016/j.febslet.2008.01.009

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title = "Transcript-specific translational regulation in the unfolded protein response of Saccharomyces cerevisiae",

abstract = "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.",

keywords = "Microarray, Polysome, Saccharomyces, Stress, Translation, UPR, Unfolded protein response",

author = "Tom Payne and Colin Hanfrey and Bishop, {Amy L.} and Michael, {Anthony J.} and Avery, {Simon V.} and Archer, {David B.}",

note = "Funding Information: We thank the Biotechnology and Biological Sciences Research Council, and Novozymes Delta Ltd., for supporting this study through a CASE studentship (IC/8675) (to T.P.). Contributory support is also acknowledged from the NIH (R01 GM57945). We thank Rohana Mat Nor for contributing Fig. 3 . ",

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doi = "10.1016/j.febslet.2008.01.009",

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AU - Payne, Tom

AU - Hanfrey, Colin

AU - Bishop, Amy L.

AU - Michael, Anthony J.

AU - Avery, Simon V.

AU - Archer, David B.

N1 - Funding Information: We thank the Biotechnology and Biological Sciences Research Council, and Novozymes Delta Ltd., for supporting this study through a CASE studentship (IC/8675) (to T.P.). Contributory support is also acknowledged from the NIH (R01 GM57945). We thank Rohana Mat Nor for contributing Fig. 3 .

PY - 2008/2/20

Y1 - 2008/2/20

N2 - 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.

AB - 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.

KW - Microarray

KW - Polysome

KW - Saccharomyces

KW - Stress

KW - Translation

KW - UPR

KW - Unfolded protein response

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

Abstract

Keywords

ASJC Scopus subject areas

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