Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings

2011 ◽  
Vol 18 (5) ◽  
pp. 564-570 ◽  
Author(s):  
Natacha Rochel ◽  
Fabrice Ciesielski ◽  
Julien Godet ◽  
Edelmiro Moman ◽  
Manfred Roessle ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Direct Repeat ◽  
Repeat Elements ◽  
Common Architecture

A genetic pathway for regulation of tra-2 translation

Development ◽  
1997 ◽  
Vol 124 (3) ◽  
pp. 749-758 ◽  
Author(s):  
E.B. Goodwin ◽  
K. Hofstra ◽  
C.A. Hurney ◽  
S. Mango ◽  
J. Kimble
Keyword(s):  
Translational Control ◽  
Direct Repeat ◽  
Postembryonic Development ◽  
Early Embryo ◽  
Translational Repression ◽  
Female Development ◽  
Normal Pattern ◽  
Repeat Elements ◽  
Translation Repression ◽  
Translational Level

In Caenorhabditis elegans, the tra-2 sex-determining gene is regulated at the translational level by two 28 nt direct repeat elements (DREs) located in its 3′ untranslated region (3′UTR). DRF is a factor that binds the DREs and may be a trans-acting translational regulator of tra-2. Here we identify two genes that are required for the normal pattern of translational control. A newly identified gene, called laf-1, is required for translational repression by the tra-2 3′UTR. In addition, the sex-determining gene, tra-3, appears to promote female development by freeing tra-2 from laf-1 repression. Finally, we show that DRF activity correlates with translational repression of tra-2 during development and that tra-3 regulates DRF activity. We suggest that tra-3 may promote female development by releasing tra-2 from translation repression by laf-1 and that translational control is important for proper sex determination--both in the early embryo and during postembryonic development.

scholarly journals The INSL3 gene is a direct target for the orphan nuclear receptor, COUP-TFII, in Leydig cells

2014 ◽  
Vol 53 (1) ◽  
pp. 43-55 ◽  
Author(s):  
Raifish E Mendoza-Villarroel ◽  
Mickaël Di-Luoffo ◽  
Etienne Camiré ◽  
Xavier C Giner ◽  
Catherine Brousseau ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Protein Interactions ◽  
Leydig Cells ◽  
Molecular Mechanisms ◽  
Direct Repeat ◽  
Testicular Descent ◽  
Mrna Levels ◽  
Orphan Nuclear Receptor ◽  
Protein Protein Interactions ◽  
Dna Precipitation

Insulin-like 3 (INSL3), a hormone produced by Leydig cells, regulates testicular descent during foetal life and bone metabolism in adults. Despite its importance, little is known about the molecular mechanisms controlling INSL3 expression. Reduced Insl3 mRNA levels were reported in the testis of mice deficient for chicken ovalbumin upstream promoter-transcription factor II (COUP-TFII), an orphan nuclear receptor known to play critical roles in cell differentiation and lineage determination in several tissues. Although COUP-TFII-deficient mice had Leydig cell dysfunction and impaired fertility, it remained unknown whether Insl3 expression was directly regulated by COUP-TFII. In this study, we observed a significant decrease in Insl3 mRNA levels in MA-10 Leydig cells depleted of COUP-TFII. Furthermore, a −1087 bp mouse Insl3 promoter was activated fourfold by COUP-TFII in MA-10 Leydig cells. Using 5′ progressive deletions, the COUP-TFII-responsive element was located between −186 and −79 bp, a region containing previously uncharacterised direct repeat 0-like (DR0-like) and DR3 elements. The recruitment and direct binding of COUP-TFII to the DR0-like element were confirmed by chromatin immunoprecipitation and DNA precipitation assay respectively. Mutation of the DR0-like element, which prevented COUP-TFII binding, significantly decreased COUP-TFII-mediated activation of the −1087 bp Insl3 reporter in CV-1 fibroblast cells but not in MA-10 Leydig cells. Finally, we found that COUP-TFII cooperates with the nuclear receptor steroidogenic factor 1 (SF1) to further enhance Insl3 promoter activity. Our results identify Insl3 as a target for COUP-TFII in Leydig cells and revealed that COUP-TFII acts through protein–protein interactions with other DNA-bound transcription factors, including SF1, to activate Insl3 transcription in these cells.

Interspecies Comparison Reveals Evolution of Control Regions in the Nematode Sex-Determining Gene tra-2

Genetics ◽  
1996 ◽  
Vol 144 (2) ◽  
pp. 597-607 ◽  
Author(s):  
Patricia E Kuwabara
Keyword(s):  
Antisense Rna ◽  
Untranslated Region ◽  
Cell Communication ◽  
Direct Repeat ◽  
Close Relative ◽  
Loss Of Function ◽  
Female Development ◽  
Repeat Elements ◽  
Alternatively Spliced ◽  
Regulatory Sites

Abstract The Caenmhabditis elegans sexdetermining gene tra-2 promotes female development and expresses 4.7-, 1.9- and 1.8-kb mRNAs. The 4.7-kb mRNA encodes the major feminizing activity of the locus, a predicted membrane receptor that mediates cell-to-cell communication, named TRA-2A. The tra-2 gene was characterized from a close relative, C. briggsae. The Cb-tra-2 gene expresses only a 4.7-kb mRNA and alternatively spliced variants, which encode TRA-2A homologues. The Cb-TRA-2A and Ce-TRA-2A sequences are highly diverged, sharing only 43% identity, although their hydropathy profiles remain remarkably similar. Three potential regulatory sites of Ce-tra-2 activity were previously identified by analyzing tra-2(eg), tra-2(gf), and tra-2(mx) mutations. Two of these sites, the EG site and MX region, are consewed in Cb-tra-2. By contrast, the two direct repeat elements in the Ce-tra-2 3′ untranslated region, which are disrupted in tra-2(gf) mutants, are absent. Injection of Cb-tra-2 antisense RNA into C. briggsae mimics the Ce-tra-2 loss-of-function phenotype. Thus, antisense RNA permits studies of gene activity in nematodes that lack extensive genetics.

A unique nuclear receptor direct repeat 17 (DR17) is present within the upstream region of Schistosoma mansoni female-specific p14 gene

2008 ◽  
Vol 371 (4) ◽  
pp. 689-693 ◽  
Author(s):  
Marcelo Rosado Fantappié ◽  
Daniel Rodrigues Furtado ◽  
Franklin David Rumjanek ◽  
Philip T. LoVerde
Keyword(s):  
Schistosoma Mansoni ◽  
Nuclear Receptor ◽  
Direct Repeat ◽  
Upstream Region ◽  
Female Specific

scholarly journals Peroxisome proliferator-activated receptors and retinoic acid receptors differentially control the interactions of retinoid X receptor heterodimers with ligands, coactivators, and corepressors.

1997 ◽  
Vol 17 (4) ◽  
pp. 2166-2176 ◽  
Author(s):  
J DiRenzo ◽  
M Söderstrom ◽  
R Kurokawa ◽  
M H Ogliastro ◽  
M Ricote ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Nuclear Receptor ◽  
Target Genes ◽  
Direct Repeat ◽  
Retinoic Acid Receptors ◽  
Structural Motif ◽  
Peroxisome Proliferator ◽  
Response Elements ◽  
Peroxisome Proliferator Activated Receptors

As the obligate member of most nuclear receptor heterodimers, retinoid X receptors (RXRs) can potentially perform two functions: cooperative binding to hormone response elements and coordinate regulation of target genes by RXR ligands. In this paper we describe allosteric interactions between RXR and two heterodimeric partners, retinoic acid receptors (RARs) and peroxisome proliferator-activated receptors (PPARs); RARs and PPARs prevent and permit activation by RXR-specific ligands, respectively. By competing for dimerization with RXR on response elements consisting of direct-repeat half-sites spaced by 1 bp (DR1 elements), the relative abundance of RAR and PPAR determines whether the RXR signaling pathway will be functional. In contrast to RAR, which prevents the binding of RXR ligands and recruits the nuclear receptor corepressor N-CoR, PPAR permits the binding of SRC-1 in response to both RXR and PPAR ligands. Overexpression of SRC-1 markedly potentiates ligand-dependent transcription by PPARgamma, suggesting that SRC-1 serves as a coactivator in vivo. Remarkably, the ability of RAR to both block the binding of ligands to RXR and interact with corepressors requires the CoR box, a structural motif residing in the N-terminal region of the RAR ligand binding domain. Mutations in the CoR box convert RAR from a nonpermissive to a permissive partner of RXR signaling on DR1 elements. We suggest that the differential recruitment of coactivators and corepressors by RAR-RXR and PPAR-RXR heterodimers provides the basis for a transcriptional switch that may be important in controlling complex programs of gene expression, such as adipocyte differentiation.

Insertional polymorphism in introns 4 and 10 of the maize ß-glucosidase gene glu1

Genome ◽  
1998 ◽  
Vol 41 (4) ◽  
pp. 597-604 ◽  
Author(s):  
Asim Esen ◽  
Hema Bandaranayake
Keyword(s):  
Inverted Repeat ◽  
Insertion Sequence ◽  
Sequence Data ◽  
Direct Repeat ◽  
Repeat Sequence ◽  
Inverted Repeat Sequence ◽  
Repeat Elements ◽  
New Family ◽  
Polymorphic Gene ◽  
Insertional Polymorphism

The major ß-glucosidase isozyme Glu1 is encoded by a highly polymorphic gene (glu1) in maize. The glu1 gene comprises 12 exons and 11 introns. Two of these introns, introns 4 and 10, show insertional polymorphism: those in allele glu1-1 (represented by inbred line OH7B) are longer than those in other inbred genotypes and in two teosintes (Zea mexicana and Zea parviglumis) surveyed. Sequence data revealed that an increase in the length of intron 4 from 150 to 477 bp in OH7B is due to a short (11 bp) tandem duplication and a large insertion sequence of 313 bp plus a 4-bp (5 ATAG 3) direct repeat. The 313-bp insertion sequence (referred to as mzsTn-1) has all the features of a transposon, having a 25-bp well-conserved (3/25 mismatches) inverted repeat sequence at its termini flanked by a 4-bp direct repeat. The increase in length from 1041 to 1302 bp in intron 10 of OH7B is due to a 259-bp insertion sequence (referred to as mzsTn-2) plus a 2-bp (5 TA 3) direct repeat. The mzsTn-2 element also possesses all the hallmarks of a transposon: a 34-bp well-conserved (3/34 mismatches) inverted repeat sequence at its termini flanked by a 2-bp direct repeat. The mzsTn-1 element belongs to a new family of inverted repeat elements, while mzsTn-2 belongs to the Stowaway family of inverted repeat elements. Analysis of PCR products from amplifications off genomic-DNA templates, using primers derived from the inverted repeat termini, and Southern blotting data suggest that both small transposons are members of a multigene family. The occurrence of two different small transposons in introns of the same glu1 allele in inbred OH7B and their absence in other genotypes suggest that they have moved into this glu1 allele recently through mediation of their autonomous counterparts that are active in OH7B or in its ancestry.Key words: ß-glucosidase, maize, intron, small transposon, polymorphism.

scholarly journals Nuclear Receptor Coactivators Facilitate Vitamin D Receptor Homodimer Action on Direct Repeat Hormone Response Elements

Endocrinology ◽  
2000 ◽  
Vol 141 (3) ◽  
pp. 1281-1284 ◽  
Author(s):  
Akira Takeshita ◽  
Yasunori Ozawa ◽  
William W. Chin
Keyword(s):  
Vitamin D ◽  
Nuclear Receptor ◽  
Vitamin D Receptor ◽  
Target Gene ◽  
Direct Repeat ◽  
Hormone Response ◽  
Mobility Shift ◽  
Response Elements ◽  
Hormone Response Elements ◽  
Nuclear Receptor Coactivators

Abstract Vitamin D receptor (VDR) is a ligand-dependent transcription factor that regulates target gene expression. Although VDR forms stable heterodimer complex with retinoid X receptors (RXRs) on vitamin D-response elements (VDREs), it is still not clear whether VDR/RXR heterodimers are the only VDR complexes responsible for vitamin D-mediated gene transcription. In this report, we analyzed the effect of nuclear receptor coactivators (SRC-1 and TRAM-1) on VDR homodimer and VDR/RXR heterodimer formation by electrophoretic mobility shift assay. We found that VDR forms stable homodimers after interaction with the coactivators on a VDRE (DR+3). Of particular note, DR+4 and DR+5 hormone-response elements (HREs) may also support such interactions. Cotransfection experiments revealed further that the coactivators enhance ligand-induced VDR transcription on these elements. Our studies suggest the important role of VDR homodimers, in addition to VDR/RXR heterodimers, in vitamin D-induced transactivation. Thus, specific coactivator-VDR interactions on HREs may determine target gene transactivation.

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