PMID- 7956930
OWN - NLM
STAT- MEDLINE
DCOM- 19941216
LR  - 20061115
IS  - 0013-7227 (Print)
IS  - 0013-7227 (Linking)
VI  - 135
IP  - 5
DP  - 1994 Nov
TI  - Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X 
      receptor-related factor.
PG  - 2076-85
AB  - 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.
FAU - Ribeiro, R C
AU  - Ribeiro RC
AD  - Metabolic Research Unit, University of California, San Francisco, California 
      94143-0540.
FAU - Apriletti, J W
AU  - Apriletti JW
FAU - Yen, P M
AU  - Yen PM
FAU - Chin, W W
AU  - Chin WW
FAU - Baxter, J D
AU  - Baxter JD
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Endocrinology
JT  - Endocrinology
JID - 0375040
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - DNA/analysis/genetics/*metabolism
MH  - Liver/chemistry/metabolism/ultrastructure
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Protein Conformation
MH  - Rats
MH  - Receptors, Cytoplasmic and Nuclear/*analysis/metabolism/*physiology
MH  - *Receptors, Retinoic Acid
MH  - Receptors, Thyroid Hormone/analysis/metabolism
MH  - Retinoid X Receptors
MH  - Transcription Factors/*analysis/metabolism/*physiology
EDAT- 1994/11/01 00:00
MHDA- 1994/11/01 00:01
CRDT- 1994/11/01 00:00
PHST- 1994/11/01 00:00 [pubmed]
PHST- 1994/11/01 00:01 [medline]
PHST- 1994/11/01 00:00 [entrez]
AID - 10.1210/endo.135.5.7956930 [doi]
PST - ppublish
SO  - Endocrinology. 1994 Nov;135(5):2076-85. doi: 10.1210/endo.135.5.7956930.