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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
1998-9-14
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pubmed:databankReference | |
pubmed:abstractText |
The pleiotropic effects of retinoids are mediated by nuclear receptors that are activated by 9-cis- or all-trans-retinoic acid to function as ligand-dependent transcription factors. In a yeast one-hybrid screen for proteins capable of interacting with native retinoic acid receptor (RAR), we have isolated the T:G mismatch-specific thymine-DNA glycosylase (TDG), which initiates the repair of T:G mismatches caused by spontaneous deamination of methylated cytosines. Here, we report that TDG can interact with RAR and the retinoid X receptor (RXR) in a ligand-independent manner, both in yeast and in vitro. Mapping of the binding sites revealed interaction with a region of the ligand binding domain harboring alpha-helix 1 in both RAR and RXR. In transient transfection experiments, TDG potentiated transactivation by RXR from a direct repeat element spaced by one nucleotide (DR1) and by RXR/RAR heterodimers from a direct repeat element spaced by five nucleotides (DR5). In vitro, TDG enhanced RXR and RXR/RAR binding to their response elements. These data indicate that TDG is not only a repair enzyme, but could also function in the control of transcription.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease (Pyrimidine Dimer),
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleic Acid Heteroduplexes,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thymine
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
273
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
20728-36
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9694815-Amino Acid Sequence,
pubmed-meshheading:9694815-Animals,
pubmed-meshheading:9694815-Base Sequence,
pubmed-meshheading:9694815-Deoxyribonuclease (Pyrimidine Dimer),
pubmed-meshheading:9694815-Endodeoxyribonucleases,
pubmed-meshheading:9694815-Guanine,
pubmed-meshheading:9694815-Mice,
pubmed-meshheading:9694815-Molecular Sequence Data,
pubmed-meshheading:9694815-Nucleic Acid Heteroduplexes,
pubmed-meshheading:9694815-Protein Binding,
pubmed-meshheading:9694815-RNA Splicing,
pubmed-meshheading:9694815-Receptors, Retinoic Acid,
pubmed-meshheading:9694815-Recombinant Proteins,
pubmed-meshheading:9694815-Sequence Homology, Amino Acid,
pubmed-meshheading:9694815-Thymine,
pubmed-meshheading:9694815-Transcriptional Activation
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pubmed:year |
1998
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pubmed:articleTitle |
Retinoic acid receptors interact physically and functionally with the T:G mismatch-specific thymine-DNA glycosylase.
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pubmed:affiliation |
Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Collège de France, BP 163, 67404 Illkirch Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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