Differential DNA binding by monomeric, homodimeric, and potentially heteromeric forms of the thyroid hormone receptor.
AUTOR(ES)
Lazar, M A
RESUMO
Binding of the thyroid hormone receptor (TR) to thyroid hormone-responsive elements (TREs) is crucial for regulation of gene expression by thyroid hormone. The TR binds to each half-site of a palindromic TRE separately, as a monomer, or simultaneously, as a homodimer. In addition, the TR monomer interacts with a 42-kDa protein that may be responsible for an increase in the apparent size and stability of the TR-TRE complex after incubation with liver nuclear extract. The multiple DNA-binding forms of the TR contact the TRE differently but compete for binding in a dynamic equilibrium which is highly dependent on the relative concentrations of TR and nuclear protein. Thus, protein-protein interactions are likely to determine the context in which the TR binds to target genes and regulates the transcriptional response to thyroid hormone.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=361489Documentos Relacionados
- Thyroid hormone receptor transcriptional activity is potentially autoregulated by truncated forms of the receptor.
- Thyroid hormone action in the absence of thyroid hormone receptor DNA-binding in vivo
- Functional dissection of the hormone and DNA binding activities of the glucocorticoid receptor.
- Ligand-binding and heterodimerization activities of a conserved region in the ligand-binding domain of the thyroid hormone receptor.
- Nucleotide sequence of cDNA encoding a novel human thyroid hormone receptor.