scholarly journals DNA hypomethylation of the nuclear receptor subfamily 5 (NR5A1) gene promoter is associated with endometriosis among women in north west of Iran

2018 ◽  
Vol 6 (1) ◽  
pp. 1-11
Author(s):  
Soraya Larki ◽  
◽  
Masoud Maleki ◽  
Keyword(s):  
Nuclear Receptor ◽  
Gene Promoter ◽  
Dna Hypomethylation ◽  
North West ◽  
Nuclear Receptor Subfamily

NR4A2 (Nuclear Receptor subfamily 4, Group a, Member 2)

2016 ◽  
pp. 1-7
Author(s):  
Floriana Volpicelli ◽  
Umberto di Porzio ◽  
Luca Colucci-D’Amato
Keyword(s):  
Nuclear Receptor ◽  
Group A ◽  
Nuclear Receptor Subfamily

A pleiotropic element in the medium-chain acyl coenzyme A dehydrogenase gene promoter mediates transcriptional regulation by multiple nuclear receptor transcription factors and defines novel receptor-DNA binding motifs

1994 ◽  
Vol 14 (7) ◽  
pp. 4360-4372
Author(s):  
M E Carter ◽  
T Gulick ◽  
D D Moore ◽  
D P Kelly
Keyword(s):  
Transcriptional Regulation ◽  
Nuclear Receptor ◽  
Receptor Binding ◽  
Gene Promoter ◽  
Response Element ◽  
Binding Motifs ◽  
Receptor Response ◽  
Dehydrogenase Gene ◽  
Chain Acyl ◽  
Acyl Coenzyme A

We previously identified a complex regulatory element in the medium-chain acyl coenzyme A dehydrogenase gene promoter that confers transcriptional regulation by the retinoid receptors RAR and RXR and the orphan nuclear receptor HNF-4. In this study we demonstrate a trans-repressing regulatory function for the orphan receptor COUP-TF at this same nuclear receptor response element (NRRE-1). The transcriptional regulatory properties and receptor binding sequences of each nuclear receptor response element within NRRE-1 are also characterized. NRRE-1 consists of four potential nuclear hormone receptor hexamer binding sites, arranged as [<--1-(n)s-2-->-3-->(n)4<--4], three of which are used in alternative pairwise binding by COUP-TF and HNF-4 homodimers and by RAR-RXR heterodimers, as demonstrated by mobility shift assays and methylation interference analysis. Binding and transactivation studies with mutant NRRE-1 elements confirmed the existence of distinct retinoid, COUP-TF, and HNF-4 response elements that define novel receptor binding motifs: COUP-TF homodimers bound sites 1 and 3 (two hexamer repeat sequences arranged as an everted imperfect repeat separated by 14 bp or ER14), RAR-RXR heterodimers bound sites 1 and 2 (ER8), and HNF-4 homodimers bound sites 2 and 3 (imperfect DR0). Mixing cotransfection experiments demonstrated that the nuclear receptor dimers compete at NRRE-1 to modulate constitutive and ligand-mediated transcriptional activity. These data suggest a mechanism for the transcriptional modulation of genes encoding enzymes involved in cellular metabolism.

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