ArticleMolecular and cellular biology2018
Transcription Activation Domains of the Yeast Factors Met4 and Ino2: Tandem Activation Domains with Properties Similar to the Yeast Gcn4 Activator.
Article in Molecular and cellular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 25 citations in OpenAlex.
- Evolutionary turnover of key amino acids explains conservation of function without conservation of sequence in transcriptional activation domains.PLoS genetics · 2026Article
- Revisiting the model for coactivator recruitment: Med15 can select its target sites independent of promoter-bound transcription factors.Nucleic acids research · 2024Article
- Alternative sulphur metabolism in the fungal pathogen Candida parapsilosis.Nature communications · 2024Article
- The Swi-Snf chromatin remodeling complex mediates gene repression through metabolic control.Nucleic acids research · 2023Article
- A Novel Mechanism of Coactivator Recruitment by the Nurr1 Nuclear Receptor.Journal of molecular biology · 2022Article
- Directed mutational scanning reveals a balance between acidic and hydrophobic residues in strong human activation domains.Cell systems · 2022Article
- Article
- Mediator subunit Med15 dictates the conserved "fuzzy" binding mechanism of yeast transcription activators Gal4 and Gcn4.Nature communications · 2021Article
- A High-Throughput Screen for Transcription Activation Domains Reveals Their Sequence Features and Permits Prediction by Deep Learning.Molecular cell · 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
- Accumulation of unacetylatable Snf2p at the INO1 promoter is detrimental to remodeler recycling supply for CUP1 induction.PloS one · 2020Article
- The Significance of the Intrinsically Disordered Regions for the Functions of the bHLH Transcription Factors.International journal of molecular sciences · 2019Review
- Proteomics Links Ubiquitin Chain Topology Change to Transcription Factor Activation.Molecular cell · 2019Article
- The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa.Molecular microbiology · 2019Article
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7 authors at 3 institutions in 1 country.
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Abstract
Eukaryotic transcription activation domains (ADs) are intrinsically disordered polypeptides that typically interact with coactivator complexes, leading to stimulation of transcription initiation, elongation, and chromatin modifications. Here we examined the properties of two strong and conserved yeast ADs: Met4 and Ino2. Both factors have tandem ADs that were identified by conserved sequence and functional studies. While the AD function of both factors depended on hydrophobic residues, Ino2 further required key conserved acidic and polar residues for optimal function. Binding studies showed that the ADs bound multiple Med15 activator-binding domains (ABDs) with similar orders of micromolar affinity and similar but distinct thermodynamic properties. Protein cross-linking data show that no unique complex was formed upon Met4-Med15 binding. Rather, we observed heterogeneous AD-ABD contacts with nearly every possible AD-ABD combination. Many of these properties are similar to those observed with yeast activator Gcn4, which forms a large heterogeneous, dynamic, and fuzzy complex with Med15. We suggest that this molecular behavior is common among eukaryotic activators.
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