Open AccessDifferential DNA binding by monomeric, homodimeric, and potentially heteromeric forms of the thyroid hormone receptor.
Author(s) -
Mitchell A. Lazar,
Thomas J. Berrodin,
Heather P. Harding
Publication year - 1991
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.11.10.5005
Subject(s) - thyroid hormone receptor , biology , thyroid hormone receptor beta , nuclear receptor , thyroid hormone receptor alpha , context (archaeology) , dna binding protein , plasma protein binding , dna , hormone response element , thyroid , hormone , binding site , receptor , biochemistry , gene , microbiology and biotechnology , hormone receptor , transcription factor , genetics , paleontology , cancer , estrogen receptor , breast cancer
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.