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The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae

Changes in cellular sterol species and concentrations can have profound effects on the transcriptional profile. In yeast, mutants defective in sterol biosynthesis show a wide range of changes in transcription, including a coinduction of anaerobic genes and ergosterol biosynthesis genes, biosynthesis...

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Autores principales: Dewhurst-Maridor, Gisèle, Abegg, Daniel, David, Fabrice P. A., Rougemont, Jacques, Scott, Cameron C., Adibekian, Alexander, Riezman, Howard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620372/
https://www.ncbi.nlm.nih.gov/pubmed/28768829
http://dx.doi.org/10.1091/mbc.E17-03-0169
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author Dewhurst-Maridor, Gisèle
Abegg, Daniel
David, Fabrice P. A.
Rougemont, Jacques
Scott, Cameron C.
Adibekian, Alexander
Riezman, Howard
author_facet Dewhurst-Maridor, Gisèle
Abegg, Daniel
David, Fabrice P. A.
Rougemont, Jacques
Scott, Cameron C.
Adibekian, Alexander
Riezman, Howard
author_sort Dewhurst-Maridor, Gisèle
collection PubMed
description Changes in cellular sterol species and concentrations can have profound effects on the transcriptional profile. In yeast, mutants defective in sterol biosynthesis show a wide range of changes in transcription, including a coinduction of anaerobic genes and ergosterol biosynthesis genes, biosynthesis of basic amino acids, and several stress genes. However the mechanisms underlying these changes are unknown. We identified mutations in the SAGA complex, a coactivator of transcription, which abrogate the ability to carry out most of these sterol-dependent transcriptional changes. In the erg3 mutant, the SAGA complex increases its occupancy time on many of the induced ergosterol and anaerobic gene promoters, increases its association with several relevant transcription factors and the SWI/SNF chromatin remodeling complex, and surprisingly, associates with an endocytic protein, Rvs167p, suggesting a moonlighting function for this protein in the sterol-regulated induction of the heat shock protein, HSP42 and HSP102, mRNAs.
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spelling pubmed-56203722017-12-16 The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae Dewhurst-Maridor, Gisèle Abegg, Daniel David, Fabrice P. A. Rougemont, Jacques Scott, Cameron C. Adibekian, Alexander Riezman, Howard Mol Biol Cell Articles Changes in cellular sterol species and concentrations can have profound effects on the transcriptional profile. In yeast, mutants defective in sterol biosynthesis show a wide range of changes in transcription, including a coinduction of anaerobic genes and ergosterol biosynthesis genes, biosynthesis of basic amino acids, and several stress genes. However the mechanisms underlying these changes are unknown. We identified mutations in the SAGA complex, a coactivator of transcription, which abrogate the ability to carry out most of these sterol-dependent transcriptional changes. In the erg3 mutant, the SAGA complex increases its occupancy time on many of the induced ergosterol and anaerobic gene promoters, increases its association with several relevant transcription factors and the SWI/SNF chromatin remodeling complex, and surprisingly, associates with an endocytic protein, Rvs167p, suggesting a moonlighting function for this protein in the sterol-regulated induction of the heat shock protein, HSP42 and HSP102, mRNAs. The American Society for Cell Biology 2017-10-01 /pmc/articles/PMC5620372/ /pubmed/28768829 http://dx.doi.org/10.1091/mbc.E17-03-0169 Text en © 2017 Dewhurst-Maridor et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Dewhurst-Maridor, Gisèle
Abegg, Daniel
David, Fabrice P. A.
Rougemont, Jacques
Scott, Cameron C.
Adibekian, Alexander
Riezman, Howard
The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae
title The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae
title_full The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae
title_fullStr The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae
title_full_unstemmed The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae
title_short The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in Saccharomyces cerevisiae
title_sort saga complex, together with transcription factors and the endocytic protein rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition in saccharomyces cerevisiae
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620372/
https://www.ncbi.nlm.nih.gov/pubmed/28768829
http://dx.doi.org/10.1091/mbc.E17-03-0169
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