Genomic organization of the human thyroid hormone receptor α (c-erbA-1) gene
- 1 January 1991
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 19 (5) , 1105-1112
- https://doi.org/10.1093/nar/19.5.1105
Abstract
The thyroid hormone receptor alpha (THRA or c-erbA-1) gene belongs to a family of genes which encode nuclear receptors for various hydrophobic ligands such as steroids, vitamin D, retinoic acid and thyroid hormones. These receptors are composed of several domains important for hormone-binding, DNA-binding, dimerization and activation of transcription. We show here that the human THRA gene is organized in 10 exons distributed along 27 kbp of genomic DNA on chromosome 17. The position of the introns in human THRA is highly conserved when compared to the chicken gene despite their differing lengths. The N-terminal A/B domain as well as the 5' untranslated region is encoded by two exons. Interestingly, each of the putative zinc fingers of the receptor DNA-binding domain is encoded by one exon and the hormone-binding domain is assembled from three exons. The two last exons of the gene are alternatively spliced to generate two different messenger RNAs. In addition, we confirm that another gene, belonging to the nuclear receptor superfamily, ear-1, overlaps with the 3' region of THRA in an opposite transcriptional orientation.Keywords
This publication has 42 references indexed in Scilit:
- Isolation of a cDNA Encoding Human Rev-ErbAα: Transcription from the Noncoding DNA Strand of a Thyroid Hormone Receptor Gene Results in a Related Protein That Does Not Bind Thyroid HormoneDNA and Cell Biology, 1990
- Expression of the v-erbA product, an altered nuclear hormone receptor, is sufficient to transform erythrocytic cells in vitroCell, 1989
- Alternative splicing generates messages encoding rat c-erbA proteins that do not bind thyroid hormone.Proceedings of the National Academy of Sciences, 1988
- Thyroid hormone receptor α isoforms generated by alternative splicing differentially activate myosin HC gene transcriptionNature, 1988
- Identification of a second human retinoic acid receptorNature, 1988
- A human retinoic acid receptor which belongs to the family of nuclear receptorsNature, 1987
- Nucleotide sequence of the chicken proto-oncogene c-erbA corresponding to domain 1 of v-erbAEuropean Journal of Biochemistry, 1987
- Expression of the v-erbA oncogene in chicken embryo fibroblasts stimulates their proliferation in vitro and enhances tumor growth in vivoCell, 1987
- Hepatitis B virus DNA integration in a sequence homologous to v-erb-A and steroid receptor genes in a hepatocellular carcinomaNature, 1986
- v-erbA cooperates with sarcoma oncogenes in leukemic cell transformationCell, 1986