+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Basal and thyroid hormone receptor auxiliary protein-enhanced binding of thyroid hormone receptor isoforms to native thyroid hormone response elements



Basal and thyroid hormone receptor auxiliary protein-enhanced binding of thyroid hormone receptor isoforms to native thyroid hormone response elements



Endocrinology 129(6): 3331-3336



There are three known isoforms of the rat thyroid hormone receptor, TR alpha-1, TR beta-1, and TR beta-2. The first two are expressed in all tissues, whereas TR beta-2 appears to be expressed only in the pituitary. The differences in the roles of the three receptor isoforms are unknown, but may involve preferential interaction with different subsets of thyroid hormone-regulated genes in different tissues. We tested the binding of the three TR isoforms to putative thyroid hormone response elements (TREs) from genes that are expressed in the pituitary or other tissues and are regulated by thyroid hormone. In vitro translated 35S-labeled rat TR alpha-1, rat TR beta-2, and human TR beta-1 receptors were bound to a battery of biotinylated synthetic deoxyribonucleotides containing naturally occurring putative TREs from genes expressed either in only pituitary (rat glycoprotein hormone alpha-subunit, TSH beta-subunit, and GH) or in nonpituitary (rat alpha-myosin heavy chain, malic enzyme, and Moloney murine leukemia virus promoter) tissues. All three receptor forms bound to each of the TREs. TR beta-2 did not show preferential binding to TREs of pituitary-specific genes compared to TR beta-1. Additionally, TR alpha-1 had a similar TRE-binding pattern as the TR beta s, except for possibly less binding to rat glycoprotein hormone alpha-subunit TRE. Finally, rat pituitary and liver nuclear extracts enhanced TR binding to TREs, with the greatest enhancement seen with the alpha-subunit TRE. These studies suggest that all TR isoforms bind similarly to native TREs. Also, TR binding to TREs can be differentially enhanced by interactions with nuclear proteins.

(PDF emailed within 0-6 h: $19.90)

Accession: 039368305

Download citation: RISBibTeXText

PMID: 1954909

DOI: 10.1210/endo-129-6-3331


Related references

Thyroid hormone response elements differentially modulate the interactions of thyroid hormone receptors with two receptor binding domains in the steroid receptor coactivator-1. Journal of Biological Chemistry 273(34): 21554-21562, 1998

Novel mode of deoxyribonucleic acid recognition by thyroid hormone receptors: thyroid hormone receptor beta-isoforms can bind as trimers to natural response elements comprised of reiterated half-sites. Molecular Endocrinology 19(1): 35-51, 2004

Half-site arrangement of hybrid glucocorticoid and thyroid hormone response elements specifies thyroid hormone receptor complex binding to DNA and transcriptional activity. Journal of Biological Chemistry 269(17): 12704-9, 1994

Relationship between P-box amino acid sequence and DNA binding specificity of the thyroid hormone receptor. The effects of sequences flanking half-sites in thyroid hormone response elements. Journal of Biological Chemistry 270(28): 16988-16994, 1995

Dna and thyroid hormone binding properties of a mutant thyroid hormone receptor c erba beta responsible for generalized thyroid hormone resistance gthr. Clinical Research 38(2): 474A, 1990

Insulin-like growth factor binding protein-6 interacts with the thyroid hormone receptor α1 and modulates the thyroid hormone-response in osteoblastic differentiation. Molecular and Cellular Biochemistry 361(1-2): 197-208, 2012

Responsiveness to thyroid hormone is enhanced in rat hepatocytes cultured as spheroids compared with that in monolayers: altered responsiveness to thyroid hormone possibly involves complex formed on thyroid hormone response elements. Thyroid 9(9): 959-967, 1999

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, 1994

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, 1994

Receptor selectivity of hormone response elements a novel thyroid hormone response element tre for thyroid hormone but not for retinoic acid receptor. Journal of Cellular Biochemistry Suppl. (14 PART B): 230, 1990

Delineation of three different thyroid hormone-response elements in promoter of rat sarcoplasmic reticulum Ca2+ATPase gene. Demonstration that retinoid X receptor binds 5' to thyroid hormone receptor in response element 1. Journal of Biological Chemistry 269(17): 13021-9, 1994

Rat Rev-erbA alpha, an orphan receptor related to thyroid hormone receptor, binds to specific thyroid hormone response elements. Molecular Endocrinology 8(3): 286-295, 1994

A dual-acceptor time-resolved Föster resonance energy transfer assay for simultaneous determination of thyroid hormone regulation of corepressor and coactivator binding to the thyroid hormone receptor: Mimicking the cellular context of thyroid hormone action. Analytical Biochemistry 386(1): 73-78, 2009

The role of thyroid hormone and thyroid hormone receptor in liver-X-receptor dependent transcriptional activation of sterol regulatory element-binding protein-1c. Diabetes 52(Suppl. 1): A318, 2003

Thyroid hormone receptor-associated proteins and general positive cofactors mediate thyroid hormone receptor function in the absence of the TATA box-binding protein-associated factors of TFIID. Proceedings of the National Academy of Sciences of the United States of America 96(5): 59-64, 1999