Thyroid hormone receptors (TR) are ligand-dependent, DNA-binding, trans-acting transcriptional factors belonging to the erbA-related steroid/thyroid hormone receptor superfamily. To better understand the structural and functional characteristics of TRs, we isolated the gene encoding human TR beta 1 (hTR beta 1). The coding region of hTR beta 1 is split into at least eight exons. Each exon well correlates with functional domains of hTR beta 1 protein, and the exon/intron organization is highly conserved when compared with the chicken c-erbA gene which encodes an alpha-type chicken TR. We demonstrate that hTR beta has at least two mRNA forms having different lengths of the 3' untranslated region. We also note several nucleotide corrections of hTR beta 1 cDNA sequence.

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