The Ets Transcription Factors Interact with Each Other and with the c-Fos/c-Jun Complex via Distinct Protein Domains in a DNA-dependent and -independent Manner
| Autor: | Elisabeth Ferreira, Giovanna Buttice, Dominique Stehelin, Jean Philippe Basuyaux |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Transcriptional Activation
Proto-Oncogene Proteins c-jun Protein domain Biochemistry c-Fos Proto-Oncogene Protein c-ets-1 chemistry.chemical_compound Transactivation ETS1 Proto-Oncogene Proteins Humans Promoter Regions Genetic Molecular Biology Transcription factor Proto-Oncogene Proteins c-ets biology c-jun DNA Cell Biology Molecular biology Gene Expression Regulation chemistry biology.protein Matrix Metalloproteinase 3 Dimerization Proto-Oncogene Proteins c-fos Erg Protein Binding Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 272:26188-26195 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.272.42.26188 |
| Popis: | The transcription factors Fos, Jun, and Ets regulate the expression of human stromelysin-1 and collagenase-1 genes. Recently, we found that ERG, an Ets family member, activates collagenase-1 gene but not stromelysin-1 by physically interacting with c-Fos/c-Jun. Interestingly, ERG binds to stromelysin-1 promoter and represses its activation by ETS2. Here, to investigate the molecular mechanism of this regulation, we have used an in vitro protein-protein interaction assay and studied the transcription factor interactions of ETS2. We found that ETS2 could weakly associate with in vitro synthesized ETS1, c-Fos, and c-Jun and strongly with c-Fos/c-Jun complex and ERG via several distinct ETS2 domains including the C-terminal region that contains the DNA-binding domain. Strikingly, these interactions were stabilized in vitro by DNA as they were inhibited by ethidium bromide. Both the N-terminal region, comprising the transactivation domain, and the C-terminal region of ETS2 associated with ERG and, interestingly, the interaction of ERG through the transactivation domain of ETS2 was DNA-independent. The DNA-dependent interaction of ETS2 with c-Fos/c-Jun was enhanced by specific DNA fragments requiring two Ets-binding sites of the stromelysin-1 promoter. Using the two hybrid system, we also demonstrated that ETS2 interacts with c-Jun or ERG in vivo. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|