In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress

Jolly, Caroline; Konecny, Lara; Grady, Deborah L.; Kutskova, Yulia A.; Cotto, José J.; Morimoto, Richard I.; Vourc’h, Claire

doi:10.1083/jcb.200109018

Cited by 136 publications

(129 citation statements)

References 36 publications

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“…Indeed, we have previously shown that HSP70 overexpression efficiently prevents the relocalization of HSF1 to the granules and the subsequent RNA polymerase II-dependent transcription of sat III repeats following heat exposure (Jolly et al, 2004). We also used a mutant of HSF1 that only contains the DNA-binding and trimerization domains (DBD+TRIM) and constitutively forms granules (Jolly et al, 2002). An interesting feature is that it acts as a dominant negative mutant, preventing the stressinduced relocalization of the endogenous HSF1 to the granules and the subsequent sat III transcription (Jolly et al, 2004).…”

Section: Resultsmentioning

confidence: 99%

A key role for stress-induced satellite III transcripts in the relocalization of splicing factors into nuclear stress granules

Metz

Soret

Vourc’h

et al. 2004

Journal of Cell Science

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116

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Exposure of cells to stressful conditions results in the rapid synthesis of a subset of specialized proteins termed heat shock proteins (HSPs) which function in protecting the cell against damage. The stress-induced activation of hsp genes is controlled by the heat shock transcription factor 1 (HSF1). At the cellular level, one of the most striking effects of stress is the rapid and reversible redistribution of HSF1 into a few nuclear structures termed nuclear stress granules which form primarily on the 9q12 locus in humans. Within these structures, HSF1 binds to satellite III repeated elements and drives the RNA polymerase II-dependent transcription of these sequences into stable RNAs which remain associated with the 9q12 locus for a certain time after synthesis. Other proteins, in particular splicing factors, were also shown to relocalize to the granules upon stress. Here, we investigated the role of stress-induced satellite III transcripts in the relocalization of splicing factors to the granules. We show that the recruitment of the two serine/arginine-rich (SR) proteins SF2/ASF and SRp30c requires the presence of stress-induced satellite III transcripts. In agreement with these findings, we identified the second RNA-recognition motif (RRM2) of hSF2/ASF as the motif required for the targeting to the granules, and we showed by immunoprecipitation that the endogenous hSF2/ASF protein is present in a complex with satellite III transcripts in stressed cells in vivo. Interestingly, satellite III transcripts also immunoprecipitate together with small nuclear ribonucleoproteins (snRNPs) in vivo whereas the intronless hsp70 transcripts do not, supporting the proposal that these transcripts are subject to splicing. Altogether, these data highlight the central role for satellite III transcripts in the targeting and/or retention of splicing factors into the granules upon stress.

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Section: Resultsmentioning

confidence: 99%

A key role for stress-induced satellite III transcripts in the relocalization of splicing factors into nuclear stress granules

Metz

Soret

Vourc’h

et al. 2004

Journal of Cell Science

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116

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“…Immunofluorescence was performed on formaldehyde-fixed cells as described previously (Jolly et al, 2002). DNA was counterstained with 250 ng/ml DAPI.…”

Section: Immunofluorescence and Microscopymentioning

confidence: 99%

Heat-Shock Factor 1 Controls Genome-wide Acetylation in Heat-shocked Cells

Fritah

Col

Boyault

et al. 2009

MBoC

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A major regulatory function has been evidenced here for HSF1, the key transcription factor of the heat-shock response, in a large-scale remodeling of the cell epigenome. Indeed, upon heat shock, HSF1, in addition to its well-known transactivating activities, mediates a genome-wide and massive histone deacetylation. Investigating the underlying mechanisms, we show that HSF1 specifically associates with and uses HDAC1 and HDAC2 to trigger this heat-shock-dependent histone deacetylation. This work therefore identifies HSF1 as a master regulator of global chromatin acetylation and reveals a cross-talk between HSF1 and histone deacetylases in the general control of genome organization in response to heat shock. INTRODUCTIONExposure of cells to environmental stress conditions results in the inducible expression of a family of proteins termed heat-shock proteins (HSPs) whose function is to protect the cells from stress-induced damages (reviewed in Lindquist¤ 1986;Christians et al., 2002). In parallel, heat shock also induces a global down-regulation of non-heat-shocked genes (Spradling et al., 1975;Jamrich et al., 1977;Findly and Pederson, 1981;Higashikubo and Roti Roti, 1993). Heatshock transcription factor 1 (HSF1) is responsible for the stress-induced activation of heat-shock genes and chromatin remodeling events associated with HSF1-mediated gene activation has been thoroughly investigated in the literature (reviewed in Wu, 1995;Sorger, 1991;Morimoto et al., 1992Morimoto et al., , 1996. In contrast, mechanisms underlying gene repression have been investigated to much lesser extent.In eukaryotic cells, the packaging of DNA into chromatin provides a dynamic structure for controlling transcription. The fundamental unit of chromatin structure, the nucleosome, is formed by a 147-base pair DNA fragment wrapped around an octamer of the four types of histones: H2A, H2B, H3 and H4, with N-terminal tails protruding from the nucleosome. Posttranslational modifications of histone tails are known to be associated with differences in gene expression (reviewed in Jenuwein and Allis, 2001;Mellor, 2006). Among other modifications, acetylation is considered as a key player in the epigenetic control of gene expression and is associated to transcriptionally active regions (reviewed in Cheung et al., 2000). The balance between opposite enzymatic activities, histone acetyl transferases (HATs), and histone deacetylases (HDACs), directly controls the level of histone acetylation and potent inhibitors of histone deacetylases, such as trichostatin A (TSA), induce a global hyperacetylation of the chromatin (Yoshida et al., 1990). Different classes of HDACs have been identified so far, with different structures and activities (reviewed in Yang and Seto, 2008). Class I and class II HDACs are classical HDACs whose activity is inhibited by TSA, whereas class III is a family of NADϩ-dependent proteins the activity of which is not affected by TSA. Only one member of class IV HDACs, HDAC11, has been identified so far. Three HDACs of class I, HDAC1...

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“…Finally, in a number of cell types, Hsf1 accumulates in a few nuclear foci during stressful events (Sarge et al 1993). These granules, termed stress granules, were found to form on chromosome 9 heterochromatin of human cells (Jolly et al 2002). It was speculated that stress granules could represent sites of storage or buffering (or both) of active Hsf1.…”

Section: Other Aspects Of Hsf-hsf1 Regulationmentioning

confidence: 99%

On mechanisms that control heat shock transcription factor activity in metazoan cells

2004

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Heat shock factor Hsf in nonvertebrate animals and homologous heat shock factor Hsf1 in vertebrate animals are key transcriptional regulators of the stress protein response. Hsf/Hsf1 is constitutively present in cells but is, typically, only active during periods during which cells are experiencing a physical or chemical proteotoxic stress. It has become increasingly clear that regulation of Hsf/Hsf1 activity occurs at multiple levels: the oligomeric status of Hsf/Hsf1, its DNA-binding ability, posttranslational modification, transcriptional competence, nuclear/ subnuclear localization, as well as its interactions with regulatory cofactors or other transcription factors all appear to be carefully controlled. This review emphasizes work reported over the past several years suggesting that regulation at several of these levels is mediated by repressive interactions of Hsp90-containing multichaperone complexes and/or individual chaperones and Hsf/Hsf1.

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In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress

Cited by 136 publications

References 36 publications

A key role for stress-induced satellite III transcripts in the relocalization of splicing factors into nuclear stress granules

A key role for stress-induced satellite III transcripts in the relocalization of splicing factors into nuclear stress granules

Heat-Shock Factor 1 Controls Genome-wide Acetylation in Heat-shocked Cells

On mechanisms that control heat shock transcription factor activity in metazoan cells

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