Specific Binding of the ETS-Domain Protein to the Interferon-Stimulated Response Element
| Autor: | Michael N. Rutherford, Bryan R.G. Williams, Aseem Kumar, S. Jaharul Haque, Jacques Ghysdael |
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| Rok vydání: | 1997 |
| Předmět: |
Molecular Sequence Data
Immunology Protein domain Response element Plasma protein binding Interferon alpha-2 Biology Proto-Oncogene Mas Gene Expression Regulation Enzymologic Proto-Oncogene Protein c-ets-1 Interferon-gamma Transcription (biology) Proto-Oncogene Proteins Virology Complementary DNA 2' 5'-Oligoadenylate Synthetase Humans Promoter Regions Genetic Cells Cultured Regulation of gene expression Base Sequence Proto-Oncogene Proteins c-ets Interferon-alpha Promoter Cell Biology Molecular biology Recombinant Proteins Stimulation Chemical Protein Structure Tertiary DNA-Binding Proteins A-site Multigene Family HeLa Cells Protein Binding Transcription Factors |
| Zdroj: | Journal of Interferon & Cytokine Research. 17:1-10 |
| ISSN: | 1557-7465 1079-9907 |
| Popis: | Interferon (IFN) activation of genes bearing an IFN-stimulated response element (ISRE) is regulated through binding of IFN-stimulated gene factors (ISGF) to the ISRE found in many IFN-stimulated genes. Using a multimerized human 2-5A synthetase ISRE as probe, we screened lambda gt11 expression libraries for cDNA encoding ISRE-binding activity and isolated a clone for murine proto-oncogene ets-1. The Ets-1 protein binds to the 2-5A synthetase ISRE at a site that also binds ISGF3, a multicomponent factor whose ISRE binding correlates with IFN-induced activation of transcription from ISRE-containing promoters. IFN-induced ISGF3 complex formation on the ISRE can be inhibited by specific Ets-1 antibody. Coexpression of Ets-1 represses ISRE-dependent reporter activity, suggesting that one or more members of the Ets protein family may negatively regulate transcriptional activity mediated by the 2-5A synthetase ISRE. |
| Databáze: | OpenAIRE |
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