ArticleNucleic acids research1996
Transactivation by the thyroid hormone receptor is dependent on the spacer sequence in hormone response elements containing directly repeated half-sites.
Article in Nucleic acids research, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- TREM2 is thyroid hormone regulated making the TREM2 pathway druggable with ligands for thyroid hormone receptor.Cell chemical biology · 2022Article
- Article
- Genome sequencing and transcriptome analyses of the Siberian hamster hypothalamus identify mechanisms for seasonal energy balance.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Thyroid Hormone Potentially Benefits Multiple Sclerosis via Facilitating Remyelination.Molecular neurobiology · 2016Review
- Ligand Independent and Subtype-Selective Actions of Thyroid Hormone Receptors in Human Adipose Derived Stem Cells.PloS one · 2016Article
- Thyroid hormone response element half-site organization and its effect on thyroid hormone mediated transcription.PloS one · 2014Article
- In-depth proteomic characterization of endogenous nuclear receptors in mouse liver.Molecular & cellular proteomics : MCP · 2013Article
- DNA recognition by thyroid hormone and retinoic acid receptors: 3,4,5 rule modified.Molecular and cellular endocrinology · 2010Article
- Liver X receptor alpha is a transcriptional repressor of the uncoupling protein 1 gene and the brown fat phenotype.Molecular and cellular biology · 2008Article
- TRIIODOTHYRONINE ACTIVATES GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 3 VIA AGGTCA-LIKE-DIRECT-REPEAT-4 TYPE THYROID HORMONE RESPONSE ELEMENT.Acta endocrinologica (Bucharest, Romania : 2005)Article
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The thyroid hormone receptor (TR) regulates the transcription of its target genes by interacting with specific hormone response elements consisting usually of directly repeated half-sites with the consensus sequence AGGTCA. To investigate the role of the spacer sequences separating the half-sites, heterodimers formed by TRalpha and the retinoid-X receptor (RXR) were used in a PCR based selection and amplification assay. The TRalpha/RXR heterodimer selected for elements with directly repeated half-sites having a spacer of 4 nucleotides (DR4). Preferences for nucleotides in the TR binding half-site motif as well as for the 4 nucleotides separating the two half-sites were found. DNA binding and transfection studies using DR4 elements with different spacer sequences showed the importance of these nucleotides for the activity of the response element: some spacer sequences allowed little or no transactivation from the element, whereas other sequences supported strong transactivation. A pyrimidine nucleotide in position three of the spacer enhanced TRalpha binding and transactivation. Additional experiments showed that heterodimers between RXR and other putative receptors exhibited a similar but distinct specificity for the spacer sequence. Our results thus suggest that the four nucleotides separating the two half-sites in hormone response elements have a major role in determining induction of hormone responsive genes.
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