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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1991-9-18
|
| pubmed:abstractText |
To assess thyroid hormone receptor (TR)-mediated activation of transcription in yeast in the presence or absence of thyroid hormone (T3), we developed a co-expression system using a TR-beta 1 expression vector and a reporter plasmid containing a 16 base pair palindromic thyroid hormone response element (TRE) upstream from a proximal CYC1 promoter that was fused to the beta-galactosidase lac Z gene of Escherichia coli. Although TR-beta 1 functions as a repressor in most mammalian systems, using our system we observed a unique thyroid hormone-independent transcriptional response indicating that wild TR-beta 1 acted as a constitutive activator in yeast; the addition of 1 microM T3 induced a moderate but significant (p less than 0.01) 25-40% further increase in transcriptional activity. Using a series of rat TR-beta 1 mutant constructs, we found that deletion of domain D and portions of E completely eliminated transcriptional activity, whereas truncations of domain F and E permitted a partial (20-40%) response compared to wild TR-beta 1 in the presence or absence of T3. These observations indicate that TR-beta 1 functions as an activator in yeast and that domains D,E and F play important interactive roles in its hormone-independent gene activation with the D domain likely being the most essential. Furthermore, our results suggest that the different transcriptional property of TR-beta 1 in yeast compared to mammalian cells i.e. activator vs repressor function, is likely determined by transcriptional factor differences which are dependent upon cellular origin.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0006-291X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
178
|
| pubmed:geneSymbol |
c-erb A
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1167-75
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:1651714-Amino Acid Sequence,
pubmed-meshheading:1651714-Animals,
pubmed-meshheading:1651714-Base Sequence,
pubmed-meshheading:1651714-Escherichia coli,
pubmed-meshheading:1651714-Gene Expression Regulation, Fungal,
pubmed-meshheading:1651714-Genes, Bacterial,
pubmed-meshheading:1651714-Genetic Vectors,
pubmed-meshheading:1651714-Liver,
pubmed-meshheading:1651714-Molecular Sequence Data,
pubmed-meshheading:1651714-Oligonucleotide Probes,
pubmed-meshheading:1651714-Promoter Regions, Genetic,
pubmed-meshheading:1651714-Proto-Oncogene Proteins,
pubmed-meshheading:1651714-Rats,
pubmed-meshheading:1651714-Receptors, Thyroid Hormone,
pubmed-meshheading:1651714-Restriction Mapping,
pubmed-meshheading:1651714-Saccharomyces cerevisiae,
pubmed-meshheading:1651714-Thyroid Hormones,
pubmed-meshheading:1651714-Transcription, Genetic,
pubmed-meshheading:1651714-Transcriptional Activation,
pubmed-meshheading:1651714-beta-Galactosidase
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Rat liver c-erb A beta 1 thyroid hormone receptor is a constitutive activator in yeast (Saccharomyces cerevisiae): essential role of domains D,E and F in hormone-independent transcription.
|
| pubmed:affiliation |
Thyroid Research Laboratory, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, University of Toronto, Ontario, Canada.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|