ArticleMolecular and cellular biology2010
Mechanism of Mediator recruitment by tandem Gcn4 activation domains and three Gal11 activator-binding domains.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- A transcription factor by any other name - function beyond DNA binding and transactivation.EMBO reports · 2026Review
- Mediator Tail Subunits Hierarchically Couple Transcriptional Condensates to Gene Activation and Genome Organization.bioRxiv : the preprint server for biology · 2026Article
- A mechanism of synergistic Mediator recruitment in RNA polymerase II transcription activation revealed by single-molecule fluorescence.Molecular cell · 2025Article
- Article
- Revisiting the model for coactivator recruitment: Med15 can select its target sites independent of promoter-bound transcription factors.Nucleic acids research · 2024Article
- Intrinsically disordered regions of the Msn2 transcription factor encode multiple functions using interwoven sequence grammars.Nucleic acids research · 2024Article
- Commonly asked questions about transcriptional activation domains.Current opinion in structural biology · 2024Review
- Broad compatibility between yeast UAS elements and core promoters and identification of promoter elements that determine cofactor specificity.Cell reports · 2023Article
- Yeast Mediator facilitates transcription initiation at most promoters via a Tail-independent mechanism.Molecular cell · 2022Article
- Suppression of p53 response by targeting p53-Mediator binding with a stapled peptide.Cell reports · 2022Article
- Ume6 Acts as a Stable Platform To Coordinate Repression and Activation of Early Meiosis-Specific Genes in Saccharomyces cerevisiae.Molecular and cellular biology · 2021Article
- Article
- Mediator subunit Med15 dictates the conserved "fuzzy" binding mechanism of yeast transcription activators Gal4 and Gcn4.Nature communications · 2021Article
- Trichoderma reesei XYR1 activates cellulase gene expression via interaction with the Mediator subunit TrGAL11 to recruit RNA polymerase II.PLoS genetics · 2020Article
- The Polymorphic PolyQ Tail Protein of the Mediator Complex, Med15, Regulates the Variable Response to Diverse Stresses.International journal of molecular sciences · 2020Article
- Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes in yeast.Nature communications · 2019Article
- The Novel ReNu Region of TAF12 Regulates Gcn5 Nucleosomal Acetylation.Journal of molecular genetics (Isleworth, London, England) · 2019Article
- Yeast AP-1 like transcription factors (Yap) and stress response: a current overview.Microbial cell (Graz, Austria) · 2019Review
- Role of integrative structural biology in understanding transcriptional initiation.Methods (San Diego, Calif.) · 2019Review
- Mediator Is Essential for Small Nuclear and Nucleolar RNA Transcription in Yeast.Molecular and cellular biology · 2018Article
2 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Targets of the tandem Gcn4 acidic activation domains in transcription preinitiation complexes were identified by site-specific cross-linking. The individual Gcn4 activation domains cross-link to three common targets, Gal11/Med15, Taf12, and Tra1, which are subunits of four conserved coactivator complexes, Mediator, SAGA, TFIID, and NuA4. The Gcn4 N-terminal activation domain also cross-links to the Mediator subunit Sin4/Med16. The contribution of the two Gcn4 activation domains to transcription was gene specific and varied from synergistic to less than additive. Gcn4-dependent genes had a requirement for Gal11 ranging from 10-fold dependence to complete Gal11 independence, while the Gcn4-Taf12 interaction did not significantly contribute to the expression of any gene studied. Complementary methods identified three conserved Gal11 activator-binding domains that bind each Gcn4 activation domain with micromolar affinity. These Gal11 activator-binding domains contribute additively to transcription activation and Mediator recruitment at Gcn4- and Gal11-dependent genes. Although we found that the conserved Gal11 KIX domain contributes to Gal11 function, we found no evidence of specific Gcn4-KIX interaction and conclude that the Gal11 KIX domain does not function by specific interaction with Gcn4. Our combined results show gene-specific coactivator requirements, a surprising redundancy in activator-target interactions, and an activator-coactivator interaction mediated by multiple low-affinity protein-protein interactions.
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