Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Ribeiro, RC; Apriletti, JW; Yen, PM; Chin, WW; Baxter, JD
Published Date
- November 1994
Published In
Volume / Issue
- 135 / 5
Start / End Page
- 2076 - 2085
PubMed ID
- 7956930
International Standard Serial Number (ISSN)
- 0013-7227
Digital Object Identifier (DOI)
- 10.1210/endo.135.5.7956930
Language
- eng
Conference Location
- United States