Dual function of a nuclear factor I binding site in MMTV transcription regulation

Autor: Elena Buetti, Blanka Kühnel, Heidi Diggelmann
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