PMID- 8288596
OWN - NLM
STAT- MEDLINE
DCOM- 19940222
LR  - 20210210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 269
IP  - 2
DP  - 1994 Jan 14
TI  - In vitro transcriptional studies of the roles of the thyroid hormone (T3) 
      response elements and minimal promoters in T3-stimulated gene transcription.
PG  - 1314-22
AB  - Thyroid hormone receptors (TRs) are ligand-dependent nuclear transcription 
      factors that are encoded by two different genes, TR alpha and TR beta, and bind 
      to thyroid hormone response elements (TREs) in the promoters of thyroid hormone 
      (T3)-regulated genes. Retinoid X receptors (RXRs), major members of the thyroid 
      hormone receptor auxiliary proteins, have recently been shown to enhance the 
      binding of TRs to TREs. We previously showed that TRs extracted from rat 
      pituitary GH3 cells retain ligand (T3) and DNA binding specificity and stimulate 
      rat growth hormone (rGH) promoter activity in a cell-free in vitro transcription 
      system. In this report, we have studied further how T3 activates endogenous TRs 
      and stimulates transcription from different TRE-containing promoters. We found 
      that T3 (10(-8) M) selectively stimulates transcription from rGH-TRE- and 
      TREpal-, but not ME-TRE- and F2-TRE-, containing templates in which these TREs 
      are linked in front of the rGH minimal promoter containing only the TATA box 
      binding protein, but not any other proximal binding protein, sequence. In 
      contrast, only the TREpal/AdML template, in which TREpal oligonucleotide was 
      linked in front of the adenovirus major late gene (AdML) minimal promoter, was 
      stimulated by T3. Electrophoretic mobility shift assay (EMSA) demonstrates that 
      endogenous TR complexes specifically bind to either natural or idealized TRE 
      (rGH-TRE, TREpal, ME-TRE, and F2-TRE) oligonucleotides. To further understand 
      these receptor-DNA complexes formed on various TREs, isoform-specific 
      anti-receptor antisera (TR alpha, TR beta 1, TR beta 2, and RXR beta) were added 
      in the EMSA. These antisera differentially supershifted TR.DNA complexes formed 
      on the TREs. These data suggest either that endogenous TR isoforms and RXR beta 
      may form different complexes on the various TREs or that TR.RXR complexes have 
      distinct conformations when bound to the various TREs. Taken together, these data 
      suggest that particular TREs in which specific TR.RXR complexes are formed and 
      different minimal promoters may provide specificity in T3-mediated 
      transcriptional stimulation of gene expression.
FAU - Suen, C S
AU  - Suen CS
AD  - Department of Medicine, Brigham and Women's Hospital, Howard Hughes Medical 
      Institute, Harvard Medical School, Boston, Massachusetts 02115.
FAU - Yen, P M
AU  - Yen PM
FAU - Chin, W W
AU  - Chin WW
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Transcription Factors)
RN  - 06LU7C9H1V (Triiodothyronine)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Cell Line
MH  - Chickens
MH  - DNA-Binding Proteins/metabolism
MH  - *Gene Expression Regulation
MH  - In Vitro Techniques
MH  - Macromolecular Substances
MH  - Molecular Sequence Data
MH  - *Promoter Regions, Genetic
MH  - Rats
MH  - Receptors, Retinoic Acid/metabolism
MH  - Receptors, Thyroid Hormone/*physiology
MH  - Transcription Factors/*physiology
MH  - *Transcription, Genetic
MH  - Triiodothyronine/*physiology
EDAT- 1994/01/14 00:00
MHDA- 1994/01/14 00:01
CRDT- 1994/01/14 00:00
PHST- 1994/01/14 00:00 [pubmed]
PHST- 1994/01/14 00:01 [medline]
PHST- 1994/01/14 00:00 [entrez]
AID - S0021-9258(17)42260-5 [pii]
PST - ppublish
SO  - J Biol Chem. 1994 Jan 14;269(2):1314-22.