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.
journal_name
Proc Natl Acad Sci U S Aauthors
Lu Z,Ansari AZ,Lu X,Ogirala A,Ptashne Mdoi
10.1073/pnas.092263499keywords:
subject
Has Abstractpub_date
2002-06-25 00:00:00pages
8591-6issue
13eissn
0027-8424issn
1091-6490pii
99/13/8591journal_volume
99pub_type
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