ArticleThe Journal of biological chemistry2008
The interaction between an acidic transcriptional activator and its inhibitor. The molecular basis of Gal4p recognition by Gal80p.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Transcription factor clusters enable target search but do not contribute to target gene activation.Nucleic acids research · 2023Article
- Transcriptional repressor Gal80 recruits corepressor complex Cyc8-Tup1 to structural genes of the Saccharomyces cerevisiae GAL regulon.Current genetics · 2022Article
- Mediator subunit Med15 dictates the conserved "fuzzy" binding mechanism of yeast transcription activators Gal4 and Gcn4.Nature communications · 2021Article
- A double role of the Gal80 N terminus in activation of transcription by Gal4p.Life science alliance · 2020Article
- The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with valines and intron reservoirs.Cellular and molecular life sciences : CMLS · 2020Article
- Electron-deficient p-benzoyl-l-phenylalanine derivatives increase covalent chemical capture yields for protein-protein interactions.Protein science : a publication of the Protein Society · 2019Article
- Assigning function to natural allelic variation via dynamic modeling of gene network induction.Molecular systems biology · 2018Article
- Phenotypic Nonspecificity as the Result of Limited Specificity of Transcription Factor Function.Genetics research international · 2018Review
- The 9aaTAD Is Exclusive Activation Domain in Gal4.PloS one · 2017Article
- Different Mechanisms Confer Gradual Control and Memory at Nutrient- and Stress-Regulated Genes in Yeast.Molecular and cellular biology · 2015Article
- Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein-protein interaction.Biopolymers · 2014Article
- Self-association of the Gal4 inhibitor protein Gal80 is impaired by Gal3: evidence for a new mechanism in the GAL gene switch.Molecular and cellular biology · 2013Article
- Regulations of sugar transporters: insights from yeast.Current genetics · 2013Review
- Ordering a dynamic protein via a small-molecule stabilizer.Journal of the American Chemical Society · 2013Article
- Interplay of a ligand sensor and an enzyme in controlling expression of the Saccharomyces cerevisiae GAL genes.Eukaryotic cell · 2012Article
- The Gal3p transducer of the GAL regulon interacts with the Gal80p repressor in its ligand-induced closed conformation.Genes & development · 2012Article
- Caught in the act: covalent cross-linking captures activator-coactivator interactions in vivo.ACS chemical biology · 2011Article
- The Cyc8-Tup1 complex inhibits transcription primarily by masking the activation domain of the recruiting protein.Genes & development · 2011Article
- Transient-state kinetic analysis of transcriptional activator·DNA complexes interacting with a key coactivator.The Journal of biological chemistry · 2011Article
- Impact of nonnatural amino acid mutagenesis on the in vivo function and binding modes of a transcriptional activator.Journal of the American Chemical Society · 2009Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The GAL genes, which encode the enzymes required for normal galactose metabolism in yeast, are transcriptionally regulated by three proteins: Gal4p, an activator; Gal80p, an inhibitor; and Gal3p, a galactose sensor. These proteins control the switch between inert and active gene expression. The transcriptional activation function of Gal4p is rendered inactive in the presence of Gal80p. Here we present the three-dimensional structure of a complex between the acidic activation domain of Gal4p and Gal80p. The transactivation domain initiates with an extended region of polypeptide chain followed by two turns of an amphipathic alpha-helix. It fits into and across a deep cleft within the Gal80p dimer with the protein-protein interface defined primarily by hydrophobic interactions. A disordered loop in the apo-Gal80p structure (Asp-309 to Ser-316) becomes well-defined upon binding of the transactivation domain. This investigation provides a new molecular scaffold for understanding previous biochemical and genetic studies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.