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The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells
One of many physiological adjustments in quiescent cells is spatial regulation of specific proteins and RNA important for the entry to or exit from the stationary phase. By examining the localization of epigenetic-related proteins in Saccharomyces cerevisiae, we observed the formation of a reversibl...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315813/ https://www.ncbi.nlm.nih.gov/pubmed/22337769 http://dx.doi.org/10.1091/mbc.E11-09-0752 |
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author | Liu, I-Chun Chiu, Sheng-Wen Lee, Hsin-Yi Leu, Jun-Yi |
author_facet | Liu, I-Chun Chiu, Sheng-Wen Lee, Hsin-Yi Leu, Jun-Yi |
author_sort | Liu, I-Chun |
collection | PubMed |
description | One of many physiological adjustments in quiescent cells is spatial regulation of specific proteins and RNA important for the entry to or exit from the stationary phase. By examining the localization of epigenetic-related proteins in Saccharomyces cerevisiae, we observed the formation of a reversible cytosolic “stationary-phase granule” (SPG) by Hos2, a nuclear histone deacetylase. In the stationary phase, hos2 mutants display reduced viability. Additionally, they exhibit a significant delay when recovering from stationary phase. Hos2 SPGs also contained Hst2, a Sir2 homologue, and several stress-related proteins, including Set3, Yca1, Hsp26, Hsp42, and some known components of stress granules. However, Hos2 SPG formation does not depend on the formation of stress granules or processing bodies. The absence or presence of glucose is sufficient to trigger assembly or disassembly of Hos2 SPGs. Among the identified components of Hos2 SPGs, Hsp42 is the first and last member observed in the Hos2 SPG assembly and disassembly processes. Hsp42 is also vital for the relocalization of the other components to Hos2 SPGs, suggesting that Hsp42 plays a central role in spatial regulation of proteins in quiescent cells. |
format | Online Article Text |
id | pubmed-3315813 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33158132012-06-16 The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells Liu, I-Chun Chiu, Sheng-Wen Lee, Hsin-Yi Leu, Jun-Yi Mol Biol Cell Articles One of many physiological adjustments in quiescent cells is spatial regulation of specific proteins and RNA important for the entry to or exit from the stationary phase. By examining the localization of epigenetic-related proteins in Saccharomyces cerevisiae, we observed the formation of a reversible cytosolic “stationary-phase granule” (SPG) by Hos2, a nuclear histone deacetylase. In the stationary phase, hos2 mutants display reduced viability. Additionally, they exhibit a significant delay when recovering from stationary phase. Hos2 SPGs also contained Hst2, a Sir2 homologue, and several stress-related proteins, including Set3, Yca1, Hsp26, Hsp42, and some known components of stress granules. However, Hos2 SPG formation does not depend on the formation of stress granules or processing bodies. The absence or presence of glucose is sufficient to trigger assembly or disassembly of Hos2 SPGs. Among the identified components of Hos2 SPGs, Hsp42 is the first and last member observed in the Hos2 SPG assembly and disassembly processes. Hsp42 is also vital for the relocalization of the other components to Hos2 SPGs, suggesting that Hsp42 plays a central role in spatial regulation of proteins in quiescent cells. The American Society for Cell Biology 2012-04-01 /pmc/articles/PMC3315813/ /pubmed/22337769 http://dx.doi.org/10.1091/mbc.E11-09-0752 Text en © 2012 Liu 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 of Cell Biology. |
spellingShingle | Articles Liu, I-Chun Chiu, Sheng-Wen Lee, Hsin-Yi Leu, Jun-Yi The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells |
title | The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells |
title_full | The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells |
title_fullStr | The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells |
title_full_unstemmed | The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells |
title_short | The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells |
title_sort | histone deacetylase hos2 forms an hsp42-dependent cytoplasmic granule in quiescent yeast cells |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315813/ https://www.ncbi.nlm.nih.gov/pubmed/22337769 http://dx.doi.org/10.1091/mbc.E11-09-0752 |
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