A target essential for the activity of a nonacidic yeast transcriptional activator.
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.
Lu
Zhen
Z
Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.
Ansari
Aseem Z
AZ
Lu
Xiangyang
X
Ogirala
Anuja
A
Ptashne
Mark
M
D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D056892:Mediator Complex; D009842:Oligopeptides / Q000378:metabolism*; D017354:Point Mutation; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D017384:Sequence Deletion; D015534:Trans-Activators / Q000235:genetics / Q000378:metabolism*
D005656:Fungal Proteins; C058337:GAL11 protein, S cerevisiae; D056892:Mediator Complex; D009842:Oligopeptides; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators