PMID- 7838157
OWN - NLM
STAT- MEDLINE
DCOM- 19950227
LR  - 20071114
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 8
IP  - 9
DP  - 1994 Sep
TI  - A chimeric thyroid hormone receptor constitutively bound to DNA requires retinoid 
      X receptor for hormone-dependent transcriptional activation in yeast.
PG  - 1245-52
AB  - T3 receptors (TRs) regulate transcription by binding to specific DNA response 
      elements as heterodimers with the retinoid X receptors (RXRs). To study the 
      consequences of this heterodimerization for transcriptional regulation in the 
      absence of complications associated with its effects on DNA binding affinity, we 
      expressed in the yeast Saccharomyces cerevisiae a chimeric protein consisting of 
      the rat TR beta 1 ligand-binding domain fused to the DNA-binding domain of the 
      bacterial repressor lexA (lexATR). LexATR is a weak, T3-responsive activator of a 
      beta-galactosidase reporter gene controlled by upstream lexA-binding sites 
      (lexA-beta-gal). In contrast, coexpression of human RXR alpha (hRXR alpha) 
      strongly enhances both the basal and ligand-induced transcriptional activities. 
      Both the N-terminal activation domain of RXR and sequences at the extreme C 
      terminus of lexATR are required for this T3- and RXR-dependent transcriptional 
      activation. The lexATR chimera was also used to characterize receptor-receptor 
      interactions using the two-hybrid system. Coexpression of B42RXR, a fusion 
      protein of the human RXR alpha ligand-binding domain and the B42 transcriptional 
      activation domain, strongly increases the transcriptional activity of lexATR in 
      the absence of T3 or 9-cis-retinoic acid. We conclude that RXR is essential for 
      full, T3-dependent transcriptional activity of the TR in yeast, and that 
      protein-protein interaction of TR and RXR in vivo is ligand-independent.
FAU - Lee, J W
AU  - Lee JW
AD  - Department of Cell Biology, Ligand Pharmaceuticals Inc, San Diego, California 
      92121.
FAU - Moore, D D
AU  - Moore DD
FAU - Heyman, R A
AU  - Heyman RA
LA  - eng
GR  - DK-43382/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (Bacterial Proteins)
RN  - 0 (LexA protein, Bacteria)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
RN  - EC 3.4.21.- (Serine Endopeptidases)
SB  - IM
GS  - lexA
MH  - Animals
MH  - Bacterial Proteins/genetics/physiology
MH  - Base Sequence
MH  - *Gene Expression Regulation, Fungal
MH  - Genes, Reporter
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Rats
MH  - Receptors, Retinoic Acid/*physiology
MH  - Receptors, Thyroid Hormone/*metabolism
MH  - Recombinant Fusion Proteins/*metabolism
MH  - Retinoid X Receptors
MH  - Saccharomyces cerevisiae/genetics/*metabolism
MH  - *Serine Endopeptidases
MH  - Transcription Factors/*physiology
MH  - *Transcription, Genetic
EDAT- 1994/09/01 00:00
MHDA- 1994/09/01 00:01
CRDT- 1994/09/01 00:00
PHST- 1994/09/01 00:00 [pubmed]
PHST- 1994/09/01 00:01 [medline]
PHST- 1994/09/01 00:00 [entrez]
AID - 10.1210/mend.8.9.7838157 [doi]
PST - ppublish
SO  - Mol Endocrinol. 1994 Sep;8(9):1245-52. doi: 10.1210/mend.8.9.7838157.