ArticleProceedings of the National Academy of Sciences of the United States of America2002
A target essential for the activity of a nonacidic yeast transcriptional activator.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with valines and intron reservoirs.Cellular and molecular life sciences : CMLS · 2020Article
- Unfolding of the C-terminal domain of the J-protein Zuo1 releases autoinhibition and activates Pdr1-dependent transcription.Journal of molecular biology · 2013Article
- Proteolytic instability and the action of nonclassical transcriptional activators.Current biology : CB · 2010Article
- Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX domain, to recruit mediator to target genes in vivo.The Journal of biological chemistry · 2010Article
- Tra1 as a screening target for transcriptional activation domain discovery.Bioorganic & medicinal chemistry letters · 2009Article
- Functional conservation of the glutamine-rich domains of yeast Gal11 and human SRC-1 in the transactivation of glucocorticoid receptor Tau 1 in Saccharomyces cerevisiae.Molecular and cellular biology · 2008Article
- H2A.Z has a function reminiscent of an activator required for preferential binding to intergenic DNA.The EMBO journal · 2003Article
- Small-molecule regulators that mimic transcription factors.Biochimica et biophysica actaReview
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Authors and funding
5 authors.
Funding
Abstract
P201 is a short (eight-residue) nonacidic peptide that comprises a strong transcriptional activating region when tethered to DNA in yeast. Here we identify the mediator protein Gal11 as an essential target of P201. Deletion of Gal11, which modestly decreases activation elicited by the typical acidic yeast activator, abolishes activation by DNA-tethered P201. A point mutation in Gal11, which has no effect on other Gal11 functions, also greatly diminishes activation by DNA-tethered P201. P201 binds to a fragment of Gal11 in vivo and in vitro, and the interaction is diminished by mutations in either component that decrease activation in vivo. P201, unlike the typical yeast acidic activating region, does not work in mammalian cells, which is consistent with the notion that the unique target of P201 (Gal11) is absent from mammalian cells.
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