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The Histone Deacetylase Hos2 Forms an Hsp42-dependent Cytoplasmic Granule in Quiescent Yeast Cells

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Journal Mol Biol Cell
Date 2012 Feb 17
PMID 22337769
Citations 34
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Abstract

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.

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References
1.
Choder M . A general topoisomerase I-dependent transcriptional repression in the stationary phase in yeast. Genes Dev. 1991; 5(12A):2315-26. DOI: 10.1101/gad.5.12a.2315. View

2.
Narayanaswamy R, Levy M, Tsechansky M, Stovall G, OConnell J, Mirrielees J . Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation. Proc Natl Acad Sci U S A. 2009; 106(25):10147-52. PMC: 2691686. DOI: 10.1073/pnas.0812771106. View

3.
Lamming D, Latorre-Esteves M, Medvedik O, Wong S, Tsang F, Wang C . HST2 mediates SIR2-independent life-span extension by calorie restriction. Science. 2005; 309(5742):1861-4. DOI: 10.1126/science.1113611. View

4.
Burtner C, Murakami C, Kennedy B, Kaeberlein M . A molecular mechanism of chronological aging in yeast. Cell Cycle. 2009; 8(8):1256-70. PMC: 2746416. DOI: 10.4161/cc.8.8.8287. View

5.
Tudisca V, Recouvreux V, Moreno S, Boy-Marcotte E, Jacquet M, Portela P . Differential localization to cytoplasm, nucleus or P-bodies of yeast PKA subunits under different growth conditions. Eur J Cell Biol. 2009; 89(4):339-48. DOI: 10.1016/j.ejcb.2009.08.005. View