ArticleThe Journal of biological chemistry2008
Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo.
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, 34 citations in OpenAlex.
- Article
- High air humidity dampens salicylic acid pathway and NPR1 function to promote plant disease.The EMBO journal · 2023Article
- Proteolytic activity of the proteasome is required for female insect reproduction.Open biology · 2021Article
- Regulation of transcriptional activators by DNA-binding domain ubiquitination.Cell death and differentiation · 2017Article
- Review
- Cullin-RING ubiquitin ligases in salicylic acid-mediated plant immune signaling.Frontiers in plant science · 2015Review
- Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.FEMS microbiology reviews · 2014Review
- Cks1 enhances transcription efficiency at the GAL1 locus by linking the Paf1 complex to the 19S proteasome.Eukaryotic cell · 2013Article
- Regulation of gene expression by the ubiquitin-proteasome system.Seminars in cell & developmental biology · 2012Review
- Ubiquitin and proteasomes in transcription.Annual review of biochemistry · 2012Review
- Mediator acts upstream of the transcriptional activator Gal4.PLoS biology · 2012Article
- Role of STRAP in regulating GSK3β function and Notch3 stabilization.Cell cycle (Georgetown, Tex.) · 2011Article
- Alterations in the interaction between GAL4 and GAL80 effect regulation of the yeast GAL regulon mediated by the F box protein Dsg1.Current microbiology · 2010Article
- Phosphorylation and ubiquitination of degron proximal residues are essential for class II transactivator (CIITA) transactivation and major histocompatibility class II expression.The Journal of biological chemistry · 2010Article
- No Splicing, no dicing: non-proteolytic roles of the ubiquitin-proteasome system in transcription.The Journal of biological chemistry · 2010Review
- The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases.Nucleic acids research · 2010Article
- Non-proteolytic regulation of p53-mediated transcription through destabilization of the activator.promoter complex by the proteasomal ATPases.The Journal of biological chemistry · 2009Article
- Proteasomal degradation of the papillomavirus E2 protein is inhibited by overexpression of bromodomain-containing protein 4.Journal of virology · 2009Article
- Phosphorylation of the Gal4 DNA-binding domain is essential for activator mono-ubiquitylation and efficient promoter occupancy.Molecular bioSystems · 2008Article
- Physical and functional interactions of monoubiquitylated transactivators with the proteasome.The Journal of biological chemistry · 2008Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae Gal4 protein is a paradigmatic transcriptional activator containing a C-terminal acidic activation domain (AD) of 34 amino acids. A mutation that results in the truncation of about two-thirds of the Gal4AD (gal4D) results in a crippled protein with only 3% the activity of the wild-type activator. We show here that although the Gal4D protein is not intrinsically deficient in DNA binding, it is nonetheless unable to stably occupy GAL promoters in vivo. This is because of the activity of the proteasomal ATPases, including Sug1/Rpt6, which bind to Gal4D via the remainder of the AD and strip it off of DNA. A mutation that suppressed the Gal4D "no growth on galactose" phenotype repressed the stripping activity of the ATPase complex but not other activities. We further demonstrate that Gal4D is hypersensitive to this stripping activity because of its failure to be monoubiquitylated efficiently in vivo and in vitro. Evidence is presented that the piece of the AD that is deleted in Gal4D protein is likely a recognition element for the E3 ubiquitin-protein ligase that modifies Gal4. These data argue that acidic ADs comprise at least two small peptide subdomains, one of which is responsible for activator monoubiquitylation and another that interacts with the proteasomal ATPases, coactivators and other transcription factors. This study validates the physiological importance of Gal4 monoubiquitylation and clarifies its major role as that of protecting the activator from being destabilized by the proteasomal ATPases.
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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.