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Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor.

Publication ,  Journal Article
Ribeiro, RC; Apriletti, JW; Yen, PM; Chin, WW; Baxter, JD
Published in: Endocrinology
November 1994

The extent thyroid hormone receptors (TRs) bind to AGGTCA-related motifs as monomers and/or homodimers, and as heterodimers with retinoid X receptors (RXRs) depends on the number, spacing, and orientation of these half-sites. Here we show that recombinant RXR alpha affects TR binding to DNA in diverse ways; it enhances recombinant TR beta 1 binding to four-nucleotide-spaced direct repeat and palindromes but not to inverted palindromes. We also used an endogenous factor termed RXR alpha-RF that cross-reacted with antibodies to RXR alpha and copurified and formed heterodimers on DNA with rat liver TRs (mostly TR beta 1 isoform), supporting the fact that endogenous TRs are commonly heterodimers. RXR alpha-RF formed, like recombinant RXR alpha, heterodimers on DNA with vitamin D and retinoic acid but not estrogen receptors. RXR alpha-RF differed from recombinant RXR alpha in that it provoked enhancement of TR beta 1 binding to DNA irrespective of half-site architecture, was resistant to heating to 50 C, and did not form heterodimers with recombinant TR alpha 2 on four-nucleotide-spaced direct repeat. The overall enhancement of TR-DNA recognition by endogenous RXR alpha-RF, not found in studies with recombinant RXR alpha, might exemplify properties acquired in vivo by endogenous RXRs; this could promote wider DNA recognition by TRs and expand the thyroid hormone transcriptional influence in the cell.

Duke Scholars

Published In

Endocrinology

DOI

ISSN

0013-7227

Publication Date

November 1994

Volume

135

Issue

5

Start / End Page

2076 / 2085

Location

United States

Related Subject Headings

  • Transcription Factors
  • Retinoid X Receptors
  • Receptors, Thyroid Hormone
  • Receptors, Retinoic Acid
  • Receptors, Cytoplasmic and Nuclear
  • Rats
  • Protein Conformation
  • Protein Binding
  • Molecular Sequence Data
  • Liver
 

Citation

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Ribeiro, R. C., Apriletti, J. W., Yen, P. M., Chin, W. W., & Baxter, J. D. (1994). Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor. Endocrinology, 135(5), 2076–2085. https://doi.org/10.1210/endo.135.5.7956930
Ribeiro, R. C., J. W. Apriletti, P. M. Yen, W. W. Chin, and J. D. Baxter. “Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor.Endocrinology 135, no. 5 (November 1994): 2076–85. https://doi.org/10.1210/endo.135.5.7956930.
Ribeiro RC, Apriletti JW, Yen PM, Chin WW, Baxter JD. Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor. Endocrinology. 1994 Nov;135(5):2076–85.
Ribeiro, R. C., et al. “Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor.Endocrinology, vol. 135, no. 5, Nov. 1994, pp. 2076–85. Pubmed, doi:10.1210/endo.135.5.7956930.
Ribeiro RC, Apriletti JW, Yen PM, Chin WW, Baxter JD. Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor. Endocrinology. 1994 Nov;135(5):2076–2085.
Journal cover image

Published In

Endocrinology

DOI

ISSN

0013-7227

Publication Date

November 1994

Volume

135

Issue

5

Start / End Page

2076 / 2085

Location

United States

Related Subject Headings

  • Transcription Factors
  • Retinoid X Receptors
  • Receptors, Thyroid Hormone
  • Receptors, Retinoic Acid
  • Receptors, Cytoplasmic and Nuclear
  • Rats
  • Protein Conformation
  • Protein Binding
  • Molecular Sequence Data
  • Liver