Cloning of an Inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1
| Autor: | Ananda L. Roy, Hong Du, Ernest Martinez, Robert G. Roeder, Carl D. Novina, Polly D. Gregor |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
DNA
Complementary Molecular Sequence Data USF1 E-box Plasma protein binding Transfection DNA-binding protein General Biochemistry Genetics and Molecular Biology Upstream Stimulatory Factor Adenoviridae Genes Reporter Transcription (biology) Humans Amino Acid Sequence Cloning Molecular Binding site Promoter Regions Genetic Molecular Biology Transcription factor Repetitive Sequences Nucleic Acid Genetics Binding Sites General Immunology and Microbiology biology General Neuroscience Recombinant Proteins Cell biology DNA-Binding Proteins Gene Expression Regulation biology.protein Upstream Stimulatory Factors HeLa Cells Protein Binding Transcription Factors Research Article |
| Zdroj: | The EMBO Journal. 16:7091-7104 |
| ISSN: | 1460-2075 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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