ArticleThe Journal of biological chemistry2010
Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX domain, to recruit mediator to target genes in vivo.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Mediator Tail Subunits Hierarchically Couple Transcriptional Condensates to Gene Activation and Genome Organization.bioRxiv : the preprint server for biology · 2026Article
- Sequence-based prediction of intermolecular interactions driven by disordered regions.Science (New York, N.Y.) · 2025Article
- Revisiting the model for coactivator recruitment: Med15 can select its target sites independent of promoter-bound transcription factors.Nucleic acids research · 2024Article
- Direct prediction of intermolecular interactions driven by disordered regions.bioRxiv : the preprint server for biology · 2024Article
- Intrinsically disordered regions of the Msn2 transcription factor encode multiple functions using interwoven sequence grammars.Nucleic acids research · 2024Article
- Inhibition of CREB Binding and Function with a Dual-Targeting Ligand.Biochemistry · 2024Article
- Differential requirements for Gcn5 and NuA4 HAT activities in the starvation-induced versus basal transcriptomes.Nucleic acids research · 2023Article
- Mediator Subunit Med15 Regulates Cell Morphology and Mating inJournal of fungi (Basel, Switzerland) · 2023Article
- Structural basis of a transcription pre-initiation complex on a divergent promoter.Molecular cell · 2023Article
- Yeast Mediator facilitates transcription initiation at most promoters via a Tail-independent mechanism.Molecular cell · 2022Article
- A Dual-Site Inhibitor of CBP/p300 KIX is a Selective and Effective Modulator of Myb.Journal of the American Chemical Society · 2021Article
- Connection of core and tail Mediator modules restrains transcription from TFIID-dependent promoters.PLoS genetics · 2021Article
- Article
- Mediator subunit Med15 dictates the conserved "fuzzy" binding mechanism of yeast transcription activators Gal4 and Gcn4.Nature communications · 2021Article
- Possible Role for Allelic Variation in YeastFrontiers in microbiology · 2021Article
- Adaptive Laboratory Evolution and Reverse Engineering of Single-Vitamin Prototrophies in Saccharomyces cerevisiae.Applied and environmental microbiology · 2020Article
- The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with valines and intron reservoirs.Cellular and molecular life sciences : CMLS · 2020Article
- The Polymorphic PolyQ Tail Protein of the Mediator Complex, Med15, Regulates the Variable Response to Diverse Stresses.International journal of molecular sciences · 2020Article
- 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
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11 authors.
Funding
Abstract
Mediator is a multisubunit coactivator required for initiation by RNA polymerase II. The Mediator tail subdomain, containing Med15/Gal11, is a target of the activator Gcn4 in vivo, critical for recruitment of native Mediator or the Mediator tail subdomain present in sin4Delta cells. Although several Gal11 segments were previously shown to bind Gcn4 in vitro, the importance of these interactions for recruitment of Mediator and transcriptional activation by Gcn4 in cells was unknown. We show that interaction of Gcn4 with the Mediator tail in vitro and recruitment of this subcomplex and intact Mediator to the ARG1 promoter in vivo involve additive contributions from three different segments in the N terminus of Gal11. These include the KIX domain, which is a critical target of other activators, and a region that shares a conserved motif (B-box) with mammalian coactivator SRC-1, and we establish that B-box is a critical determinant of Mediator recruitment by Gcn4. We further demonstrate that Gcn4 binds to the Gal11 KIX domain directly and, by NMR chemical shift analysis combined with mutational studies, we identify the likely binding site for Gcn4 on the KIX surface. Gcn4 is distinctive in relying on comparable contributions from multiple segments of Gal11 for efficient recruitment of Mediator in vivo.
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