A T-cell protein which recognizes a palindromic DNA sequence in the negative regulatory element of the HIV-1 long terminal repeat with homology to steroid/thyroid hormone receptor binding sites

1990 ◽  
Vol 18 (4) ◽  
pp. 555-556 ◽  
Author(s):  
KIM ORCHARD ◽  
NEIL PERKINS ◽  
CAROLINE CHAPMAN ◽  
JULIAN HARRIS ◽  
VINCENT EMERY ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Dna Sequence ◽  
Receptor Binding ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Regulatory Element ◽  
Cell Protein ◽  
Negative Regulatory Element ◽  
Hiv 1

scholarly journals Modular Insulators: Genome Wide Search for Composite CTCF/Thyroid Hormone Receptor Binding Sites

PLoS ONE ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. e10119 ◽  
Author(s):  
Oliver Weth ◽  
Christine Weth ◽  
Marek Bartkuhn ◽  
Joerg Leers ◽  
Florian Uhle ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Receptor Binding ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Genome Wide ◽  
Genome Wide Search

scholarly journals Identification of Thyroid Hormone Receptor Binding Sites and Target Genes Using ChIP-on-Chip in Developing Mouse Cerebellum

PLoS ONE ◽  
2009 ◽  
Vol 4 (2) ◽  
pp. e4610 ◽  
Author(s):  
Hongyan Dong ◽  
Carole L. Yauk ◽  
Andrea Rowan-Carroll ◽  
Seo-Hee You ◽  
R. Thomas Zoeller ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Receptor Binding ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Target Genes ◽  
Thyroid Hormone Receptor ◽  
Mouse Cerebellum ◽  
On Chip

scholarly journals Identification of thyroid hormone receptor binding sites in developing mouse cerebellum

BMC Genomics ◽  
2013 ◽  
Vol 14 (1) ◽  
pp. 341 ◽  
Author(s):  
Remi Gagne ◽  
James R Green ◽  
Hongyan Dong ◽  
Mike G Wade ◽  
Carole L Yauk
Keyword(s):  
Thyroid Hormone ◽  
Receptor Binding ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Mouse Cerebellum

scholarly journals Novel Mechanism of Positive versus Negative Regulation by Thyroid Hormone Receptor β1 (TRβ1) Identified by Genome-wide Profiling of Binding Sites in Mouse Liver

2013 ◽  
Vol 289 (3) ◽  
pp. 1313-1328 ◽  
Author(s):  
Preeti Ramadoss ◽  
Brian J. Abraham ◽  
Linus Tsai ◽  
Yiming Zhou ◽  
Ricardo H. Costa-e-Sousa ◽  
...  
Keyword(s):  
Gene Expression ◽  
Transcriptional Regulation ◽  
Thyroid Hormone ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Target Genes ◽  
Thyroid Hormone Receptor ◽  
Negative Regulation ◽  
Genome Wide

Triiodothyronine (T3) regulates key metabolic processes in the liver through the thyroid hormone receptor, TRβ1. However, the number of known target genes directly regulated by TRβ1 is limited, and the mechanisms by which positive and especially negative transcriptional regulation occur are not well understood. To characterize the TRβ1 cistrome in vivo, we expressed a biotinylated TRβ1 in hypo- and hyperthyroid mouse livers, used ChIP-seq to identify genomic TRβ1 targets, and correlated these data with gene expression changes. As with other nuclear receptors, the majority of TRβ1 binding sites were not in proximal promoters but in the gene body of known genes. Remarkably, T3 can dictate changes in TRβ1 binding, with strong correlation to T3-induced gene expression changes, suggesting that differential TRβ1 binding regulates transcriptional outcome. Additionally, DR-4 and DR-0 motifs were significantly enriched at binding sites where T3 induced an increase or decrease in TRβ1 binding, respectively, leading to either positive or negative regulation by T3. Taken together, the results of this study provide new insights into the mechanisms of transcriptional regulation by TRβ1 in vivo.

Thyroid hormone receptor β mRNA expression in Sertoli cells isolated from prepubertal testis

1995 ◽  
Vol 14 (1) ◽  
pp. 131-134 ◽  
Author(s):  
S Palmero ◽  
P De Marco ◽  
E Fugassa
Keyword(s):  
Polymerase Chain Reaction ◽  
Thyroid Hormone ◽  
Sertoli Cell ◽  
Sertoli Cells ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Chain Reaction ◽  
Polymerase Chain ◽  
Thyroid Hormone Receptor Β

ABSTRACT A polymerase chain reaction (PCR)-based assay was used to evaluate the expression of thyroid hormone receptor β mRNA in Sertoli cells isolated from both prepubertal rat and piglet testes. The expression of an mRNA coding for the functional thyroid hormone receptor β isoform, as established by the PCR assay, agrees with the presence of specific tri-iodothyronine (T3)-binding sites in the Sertoli cell nuclei of both species, as previously evaluated by displacement analysis. The results ratify the existence of a functional T3 receptor in the prepubertal testis and confirm the Sertoli cell as a specific target for thyroid hormone action on the developing testis. On the other hand, in both peripubertal rat (Palmero et al. 1988; Jannini et al. 1990) and piglet (Palmero et al. 1992) testes, high-affinity, low-capacity T3 binding sites have been specifically localised at the Sertoli cell level and TRal mRNA expression has been detected very recently in immature Sertoli cells (Jannini et al. 1994). The aim of the present work was to test if, in prepubertal Sertoli cells isolated from both immature rat and piglet testes, the expression of an erbAβ mRNA specifically coding for the TR protein could be detected employing an highly sensitive polymerase chain reaction (PCR)-based assay.

scholarly journals Myocyte-specific enhancer factor 2 and thyroid hormone receptor associate and synergistically activate the alpha-cardiac myosin heavy-chain gene.

1997 ◽  
Vol 17 (5) ◽  
pp. 2745-2755 ◽  
Author(s):  
Y Lee ◽  
B Nadal-Ginard ◽  
V Mahdavi ◽  
S Izumo
Keyword(s):  
Thyroid Hormone ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Physical Interaction ◽  
Cardiac Myosin ◽  
Nonmuscle Cells ◽  
Enhancer Factor

The muscle-specific regulatory region of the alpha-cardiac myosin heavy-chain (MHC) gene contains the thyroid hormone response element (TRE) and two A/T-rich DNA sequences, designated A/T1 and A/T2, the putative myocyte-specific enhancer factor 2 (MEF2) binding sites. We investigated the roles of the TRE and MEF2 binding sites and the potential interaction between thyroid hormone receptor (TR) and MEF2 proteins regulating the alpha-MHC promoter. Deletion mutation analysis indicated that both the A/T2 motif and TRE were required for muscle-specific expression of the alpha-MHC gene. The alpha-MHC enhancer containing both the A/T2 motif and TRE was synergistically activated by coexpression of MEF2 and TR in nonmuscle cells, whereas neither factor by itself activated the alpha-MHC reporters. The reporter construct containing the A/T2 sequence and the TRE linked to a heterologous promoter also showed synergistic activation by coexpression of MEF2 and TR in nonmuscle cells. Moreover, protein binding assays demonstrated that MEF2 and TR specifically bound to one another in vitro and in vivo. The MADS domain of MEF2 and the DNA-binding domain of TR were necessary and sufficient to mediate their physical interaction. Our results suggest that the members of the MADS family (MEF2) and steroid receptor superfamily (TR) interact with one another to synergistically activate the alpha-cardiac MHC gene expression.

scholarly journals A TNF Variant that Associates with Susceptibility to Musculoskeletal Disease Modulates Thyroid Hormone Receptor Binding to Control Promoter Activation

PLoS ONE ◽  
2013 ◽  
Vol 8 (9) ◽  
pp. e76034 ◽  
Author(s):  
Endre Kiss-Toth ◽  
Edward Harlock ◽  
Darren Lath ◽  
Thomas Quertermous ◽  
J. Mark Wilkinson
Keyword(s):  
Thyroid Hormone ◽  
Receptor Binding ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Musculoskeletal Disease ◽  
Promoter Activation
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