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Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers.

Publication ,  Journal Article
Yen, PM; Darling, DS; Carter, RL; Forgione, M; Umeda, PK; Chin, WW
Published in: J Biol Chem
February 25, 1992

Thyroid hormone receptors (TRs) are ligand-dependent transcription factors that bind to thyroid hormone response elements (TREs) to mediate positive and negative regulation of transcription of thyroid hormone-responsive genes. TR binding to TREs can be enhanced by interaction with a nuclear protein, triiodothyronine (T3) receptor auxiliary protein (TRAP). There are two major isoforms of thyroid hormone receptors, TR alpha-1 and TR beta-1, which are encoded on two separate genes. We studied the binding of TR alpha-1 and TR beta-1 to several TREs: the chick lysozyme TRE (F2), which is positively regulated by T3; rabbit beta-myosin heavy chain TRE, which is negatively regulated by T3; and an idealized inverted palindrome, TRElap. We demonstrate the formation of homodimers, TR alpha/TR beta dimers, and TR/TRAP heterodimers when receptor is bound to these DNA sequences. Surprisingly, we found that T3 decreased TR alpha-1 and TR beta-1 homodimer binding in a dose-dependent manner to these TREs as well as TR alpha/TR beta dimer binding to F2. In contrast, T3 did not affect TR/TRAP heterodimer binding to TREs suggesting that this heterodimer may be the stable complex occupying TREs in the presence of ligand.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

February 25, 1992

Volume

267

Issue

6

Start / End Page

3565 / 3568

Location

United States

Related Subject Headings

  • Triiodothyronine
  • Transcription, Genetic
  • Receptors, Thyroid Hormone
  • Rats
  • Protein Binding
  • Myosins
  • Muramidase
  • Humans
  • Gene Expression Regulation
  • Electrophoresis
 

Citation

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Yen, P. M., Darling, D. S., Carter, R. L., Forgione, M., Umeda, P. K., & Chin, W. W. (1992). Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers. J Biol Chem, 267(6), 3565–3568.
Yen, P. M., D. S. Darling, R. L. Carter, M. Forgione, P. K. Umeda, and W. W. Chin. “Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers.J Biol Chem 267, no. 6 (February 25, 1992): 3565–68.
Yen PM, Darling DS, Carter RL, Forgione M, Umeda PK, Chin WW. Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers. J Biol Chem. 1992 Feb 25;267(6):3565–8.
Yen, P. M., et al. “Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers.J Biol Chem, vol. 267, no. 6, Feb. 1992, pp. 3565–68.
Yen PM, Darling DS, Carter RL, Forgione M, Umeda PK, Chin WW. Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers. J Biol Chem. 1992 Feb 25;267(6):3565–3568.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

February 25, 1992

Volume

267

Issue

6

Start / End Page

3565 / 3568

Location

United States

Related Subject Headings

  • Triiodothyronine
  • Transcription, Genetic
  • Receptors, Thyroid Hormone
  • Rats
  • Protein Binding
  • Myosins
  • Muramidase
  • Humans
  • Gene Expression Regulation
  • Electrophoresis