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Thyroid hormone receptor monomer, homodimer, and heterodimer (with retinoid-X receptor) contact different nucleotide sequences in thyroid hormone response elements


Thyroid hormone receptor monomer, homodimer, and heterodimer (with retinoid-X receptor) contact different nucleotide sequences in thyroid hormone response elements



Endocrinology 135(4): 1628-1638



ISSN/ISBN: 0013-7227

PMID: 7925126

DOI: 10.1210/en.135.4.1628

Thyroid hormone receptors (TRs) bind as monomers, homodimers, and heterodimers with nuclear proteins such as retinoid-X receptors (RXRs) to thyroid hormone response elements (TREs). However, it is not known which nucleotides each TR complex contacts in a particular TRE. To identify the precise contact sites on a synthetic DR4 (TRE half-sites arranged as a direct repeat with a four-nucleotide spacer) and a chick lysoenzyme TRE, F2 (half-sites arranged as an inverted palindrome with a six-nucleotide spacer), for various TR complexes, mobility shift assays, and dimethylsulfate and KMnO-4 DNA modification interference assays were employed. First, TR-alpha monomer bound to the downstream half-site of these TREs, whereas TR-alpha homodimer bound to both half-sites. TR-alpha/RXR-alpha heterodimer also bound to both half-sites, but "preferred" to contact the down-stream half-site. Second, the specific flanking and spacing sequences of DR4 influenced the contact sites and the binding of TR-alpha monomer and homodimer, but not TR-alpha/RXR-alpha heterodimer. Finally, cotransfection studies, using reporter plasmids containing DR4 or F2 in both orientations with respect to the basal promoter, provide evidence that preferential contact with the down-stream half-site by TR/RXR heterodimer may be important for maximal transcriptional activation.

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