ArticleThe Journal of biological chemistry2013
Mediator recruitment to heat shock genes requires dual Hsf1 activation domains and mediator tail subunits Med15 and Med16.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- MED26 facilitates Mediator-Pol II complex assembly and promotes nuclear stress body formation during heat stress.iScience · 2026Article
- Emergent 3D genome reorganization and graded gene control from the stepwise assembly of transcriptional condensates.Cell reports · 2026Article
- A phosphatidic acid-based retrograde signaling pathway responsive to abiotic stress in Arabidopsis.The Plant journal : for cell and molecular biology · 2026Article
- Mediator Tail Subunits Hierarchically Couple Transcriptional Condensates to Gene Activation and Genome Organization.bioRxiv : the preprint server for biology · 2026Article
- Conservation of mRNA operon formation in control of the heat shock response in mammalian cells.Science advances · 2025Article
- Real-time visualization of reconstituted transcription reveals RNAPII activation mechanisms at single promoters.Cell reports · 2025Article
- Nuclear basket proteins Nup2 and Mlp1 drive heat shock-induced 3D genome restructuring downstream of transcriptional activation.The Journal of biological chemistry · 2025Article
- Nuclear basket proteins Nup2 and Mlp1 drive heat shock-induced 3D genome restructuring downstream of transcriptional activation.bioRxiv : the preprint server for biology · 2025Article
- Editorial: Survival strategies: cellular responses to stress and damage.Frontiers in cell and developmental biology · 2025Article
- Article
- Moesin contributes to heat shock gene response through direct binding to the Med15 subunit of the Mediator complex in the nucleus.Open biology · 2024Article
- Heat Shock Factor 1 forms nuclear condensates and restructures the yeast genome before activating target genes.bioRxiv : the preprint server for biology · 2024Article
- The Heat Shock Response as a Condensate Cascade.Journal of molecular biology · 2024Review
- LowTempGAL: a highly responsive low temperature-inducible GAL system in Saccharomyces cerevisiae.Nucleic acids research · 2024Article
- Inducible transcriptional condensates drive 3D genome reorganization in the heat shock response.Molecular cell · 2022Article
- An Important Role for RPRD1B in the Heat Shock Response.Molecular and cellular biology · 2022Article
- Phase-separation antagonists potently inhibit transcription and broadly increase nucleosome density.The Journal of biological chemistry · 2022Article
- An integrated SAGA and TFIID PIC assembly pathway selective for poised and induced promoters.Genes & development · 2022Article
- HSF1 phosphorylation establishes an active chromatin state via the TRRAP-TIP60 complex and promotes tumorigenesis.Nature communications · 2022Article
- Whole-Genome Analyses Reveal Genomic Characteristics and Selection Signatures of Lincang Humped Cattle at the China-Myanmar Border.Frontiers in genetics · 2022Article
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The evolutionarily conserved Mediator complex is central to the regulation of gene transcription in eukaryotes because it serves as a physical and functional interface between upstream regulators and the Pol II transcriptional machinery. Nonetheless, its role appears to be context-dependent, and the detailed mechanism by which it governs the expression of most genes remains unknown. Here we investigate Mediator involvement in HSP (heat shock protein) gene regulation in the yeast Saccharomyces cerevisiae. We find that in response to thermal upshift, subunits representative of each of the four Mediator modules (Head, Middle, Tail, and Kinase) are rapidly, robustly, and selectively recruited to the promoter regions of HSP genes. Their residence is transient, returning to near-background levels within 90 min. Hsf1 (heat shock factor 1) plays a central role in recruiting Mediator, as indicated by the fact that truncation of either its N- or C-terminal activation domain significantly reduces Mediator occupancy, whereas removal of both activation domains abolishes it. Likewise, ablation of either of two Mediator Tail subunits, Med15 or Med16, reduces Mediator recruitment to HSP promoters, whereas deletion of both abolishes it. Accompanying the loss of Mediator, recruitment of RNA polymerase II is substantially diminished. Interestingly, Mediator antagonizes Hsf1 occupancy of non-induced promoters yet facilitates enhanced Hsf1 association with activated ones. Collectively, our observations indicate that Hsf1, via its dual activation domains, recruits holo-Mediator to HSP promoters in response to acute heat stress through cooperative physical and/or functional interactions with the Tail module.
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