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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.

Original publication

DOI

10.1073/pnas.092263499

Type

Journal article

Journal

Proc Natl Acad Sci U S A

Publication Date

25/06/2002

Volume

99

Pages

8591 - 8596

Keywords

Fungal Proteins, Mediator Complex, Oligopeptides, Point Mutation, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Deletion, Trans-Activators