| First Author | Um S | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 33 | Pages | 20728-36 |
| PubMed ID | 9694815 | Mgi Jnum | J:52013 |
| Mgi Id | MGI:1327703 | Doi | 10.1074/jbc.273.33.20728 |
| Citation | Um S, et al. (1998) Retinoic acid receptors interact physically and functionally with the T:G mismatch-specific thymine-DNA glycosylase. J Biol Chem 273(33):20728-36 |
| 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. |
