Dual function of a nuclear factor I binding site in MMTV transcription regulation
Autor: | Elena Buetti, Blanka Kühnel, Heidi Diggelmann |
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Rok vydání: | 1989 |
Předmět: |
Transcription
Genetic TATA box DNA Mutational Analysis Cooperativity Regulatory Sequences Nucleic Acid Biology Dexamethasone Mice L Cells Receptors Glucocorticoid Glucocorticoid receptor Animals Binding Sites *CCAAT-Enhancer-Binding Proteins DNA Mutational Analysis DNA-Binding Proteins/*physiology Dexamethasone/pharmacology Gene Expression Regulation/drug effects L Cells (Cell Line) Mammary Tumor Virus Mouse/*genetics Mice NFI Transcription Factors Nuclear Proteins/*physiology *Promoter Regions (Genetics) Receptors Glucocorticoid/physiology *Regulatory Sequences Nucleic Acid Transcription Factors/*physiology Transcription Genetic Y-Box-Binding Protein 1 Genetics Animals Binding site Promoter Regions Genetic Transcription factor Binding Sites Nuclear factor I Mouse mammary tumor virus Nuclear Proteins Y box binding protein 1 biology.organism_classification Molecular biology DNA-Binding Proteins NFI Transcription Factors Gene Expression Regulation Mammary Tumor Virus Mouse CCAAT-Enhancer-Binding Proteins Y-Box-Binding Protein 1 Transcription Factors |
Zdroj: | Nucleic Acids Research, vol. 17, no. 8, pp. 3065-78 |
ISSN: | 1362-4962 0305-1048 |
DOI: | 10.1093/nar/17.8.3065 |
Popis: | Using linker-scanning mutagenesis we had previously identified four elements within the MMTV LTR which are necessary for transcriptional stimulation by glucocorticoid hormones. Two of them overlapped with regions to which the glucocorticoid receptor binds in vitro. The third element contained a NF-I binding site, and the fourth the TATA box. Here we show that mutations that abolish in vitro binding of NF-I had a negative effect also on the basal activity of the MMTV promoter of LTR-containing plasmids stably integrated in Ltk- fibroblasts. The analysis of double mutants altered in the NF-I plus either one of the receptor binding elements further demonstrated that the NF-I site functionally cooperated with the proximal (-120) element, which alone was extremely inefficient in stimulation. The stronger distal (-181/-172) element was independent of NF-I and showed functional cooperativity with the proximal hormone-binding element. |
Databáze: | OpenAIRE |
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