Source:http://linkedlifedata.com/resource/pubmed/id/11478808
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2001-7-31
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pubmed:abstractText |
The human TR4 orphan receptor (TR4) is a member of the nuclear receptor superfamily. It functions as a transcriptional factor which regulates and controls many important physiological functions. It has been documented that TR4 may bind as a homodimer to a DNA response element containing two direct repeats of the AGGTCA consensus motif. Surprisingly, our data reveal that the expression of the human steroid 21-hydroxylase (21-OHase) gene could be repressed by TR4 via the monomeric AGGTCA motif (-228TR4RE) at its 5' flanking region (nucleotide numbers 1431-1444, 5'-GGAAAAAGGTCAGG-3'). Electrophoretic mobility shift assay showed specific binding with a dissociation constant of 0.4 nM between TR4 and the monomeric -288TR4RE motif. However, TR4 does not form heterodimers with either retinoid X receptor alpha or SHP (short heterodimer partner) orphan receptor. Additionally, both dual-luciferase and chloramphenicol acetyltransferase assays demonstrated that TR4 can function as a repressor via the -228TR4RE of the 21-OHase gene. In conclusion, our data suggest that TR4 may bind to a monomeric DNA response element and play an important role in the suppression of the 21-OHase gene expression.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5' Untranslated Regions,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/NR2C2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Steroid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid 21-Hydroxylase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1361-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11478808-5' Untranslated Regions,
pubmed-meshheading:11478808-Amino Acid Motifs,
pubmed-meshheading:11478808-Binding, Competitive,
pubmed-meshheading:11478808-DNA,
pubmed-meshheading:11478808-Dimerization,
pubmed-meshheading:11478808-Gene Expression Regulation,
pubmed-meshheading:11478808-Humans,
pubmed-meshheading:11478808-Nerve Tissue Proteins,
pubmed-meshheading:11478808-Protein Binding,
pubmed-meshheading:11478808-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:11478808-Receptors, Steroid,
pubmed-meshheading:11478808-Receptors, Thyroid Hormone,
pubmed-meshheading:11478808-Response Elements,
pubmed-meshheading:11478808-Steroid 21-Hydroxylase,
pubmed-meshheading:11478808-Substrate Specificity
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pubmed:year |
2001
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pubmed:articleTitle |
TR4 orphan receptor represses the human steroid 21-hydroxylase gene expression through the monomeric AGGTCA motif.
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pubmed:affiliation |
Institute of Biotechnology, National Dong Hwa University, Hualien, Taiwan, 974, Republic of China. hjlee@mail.ndhu.edu.tw
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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