ArticleThe Journal of biological chemistry2009
SAGA and Rpd3 chromatin modification complexes dynamically regulate heat shock gene structure and expression.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 55 citations in OpenAlex.
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- Isoform-specific cofactor recruitment through the intrinsically disordered N-terminus of p63 underlies differential transcriptional activities.bioRxiv : the preprint server for biology · 2026Article
- Characterization of Transcriptional, Epigenetic, and Phenotypic Plasticity and Discovery of Biomarkers in Acute and Chronic Murine Schistosomiasis Infection.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Article
- Heat Shock Factor 1 forms nuclear condensates and restructures the yeast genome before activating target genes.bioRxiv : the preprint server for biology · 2024Article
- Diverse yeast antiviral systems prevent lethal pathogenesis caused by the L-A mycovirus.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Phase-separation antagonists potently inhibit transcription and broadly increase nucleosome density.The Journal of biological chemistry · 2022Article
- DNA circles promote yeast ageing in part through stimulating the reorganization of nuclear pore complexes.eLife · 2022Article
- Primordial super-enhancers: heat shock-induced chromatin organization in yeast.Trends in cell biology · 2021Review
- Actin R256 Mono-methylation Is a Conserved Post-translational Modification Involved in Transcription.Cell reports · 2020Article
- Dynamic modules of the coactivator SAGA in eukaryotic transcription.Experimental & molecular medicine · 2020Review
- Varying Architecture of Heat Shock Elements Contributes to Distinct Magnitudes of Target Gene Expression and Diverged Biological Pathways in Heat Stress Response of Bread Wheat.Frontiers in genetics · 2020Article
- Genetic and epigenetic determinants establish a continuum of Hsf1 occupancy and activity across the yeast genome.Molecular biology of the cell · 2018Article
- Heat Shock Protein Genes Undergo Dynamic Alteration in Their Three-Dimensional Structure and Genome Organization in Response to Thermal Stress.Molecular and cellular biology · 2017Article
- Cooperation between SAGA and SWI/SNF complexes is required for efficient transcriptional responses regulated by the yeast MAPK Slt2.Nucleic acids research · 2016Article
- Evidence for Multiple Mediator Complexes in Yeast Independently Recruited by Activated Heat Shock Factor.Molecular and cellular biology · 2016Article
- A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions.Molecular & cellular proteomics : MCP · 2014Article
- Uncoupling transcription from covalent histone modification.PLoS genetics · 2014Article
- The yeast Snt2 protein coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress.Molecular and cellular biology · 2013Article
- Photoperiodic regulation of flowering time through periodic histone deacetylation of the florigen gene FT.PLoS biology · 2013Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chromatin structure of heat shock protein (HSP)-encoding genes undergoes dramatic alterations upon transcriptional induction, including, in extreme cases, domain-wide nucleosome disassembly. Here, we use a combination of gene knock-out, in situ mutagenesis, chromatin immunoprecipitation, and expression assays to investigate the role of histone modification complexes in regulating heat shock gene structure and expression in Saccharomyces cerevisiae. Two histone acetyltransferases, Gcn5 and Esa1, were found to stimulate HSP gene transcription. A detailed chromatin immunoprecipitation analysis of the Gcn5-containing SAGA complex (signified by Spt3) revealed its presence within the promoter of every heat shock factor 1-regulated gene examined. The occupancy of SAGA increased substantially upon heat shock, peaking at several HSP promoters within 30-45 s of temperature upshift. SAGA was also efficiently recruited to the coding regions of certain HSP genes (where its presence mirrored that of pol II), although not at others. Robust and rapid recruitment of repressive, Rpd3-containing histone deacetylase complexes was also seen and at all HSP genes examined. A detailed analysis of HSP82 revealed that both Rpd3(L) and Rpd3(S) complexes (signified by Sap30 and Rco1, respectively) were recruited to the gene promoter, yet only Rpd3(S) was recruited to its open reading frame. A consensus URS1 cis-element facilitated the recruitment of each Rpd3 complex to the HSP82 promoter, and this correlated with targeted deacetylation of promoter nucleosomes. Collectively, our observations reveal that SAGA and Rpd3 complexes are rapidly and synchronously recruited to heat shock factor 1-activated genes and suggest that their opposing activities modulate heat shock gene chromatin structure and fine-tune transcriptional output.
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