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- Title
Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1.
- Authors
Roy, A L; Du, H; Gregor, P D; Novina, C D; Martinez, E; Roeder, R G
- Abstract
The transcription factor TFII-I has been shown to bind independently to two distinct promoter elements, a pyrimidine-rich initiator (Inr) and a recognition site (E-box) for upstream stimulatory factor 1 (USF1), and to stimulate USF1 binding to both of these sites. Here we describe the isolation of a cDNA encoding TFII-I and demonstrate that the corresponding 120 kDa polypeptide, when expressed ectopically, is capable of binding to both Inr and E-box elements. The primary structure of TFII-I reveals novel features that include six directly repeated 90 residue motifs that each possess a potential helix-loop/span-helix homology. These unique structural features suggest that TFII-I may have the capacity for multiple protein-protein and, potentially, multiple protein-DNA interactions. Consistent with this hypothesis and with previous in vitro studies, we further demonstrate that ectopic TFII-I and USF1 can act synergistically, and in some cases independently, to activate transcription in vivo through both Inr and the E-box elements of the adenovirus major late promoter. We also describe domains of USF1 that are necessary for its independent and synergistic activation functions.
- Publication
The EMBO journal, 1997, Vol 16, Issue 23, p7091
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/16.23.7091