Retinoic acid receptors interact physically and functionally with the T:G mismatch-specific thymine-DNA glycosylase.
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.[1]References
- Retinoic acid receptors interact physically and functionally with the T:G mismatch-specific thymine-DNA glycosylase. Um, S., Harbers, M., Benecke, A., Pierrat, B., Losson, R., Chambon, P. J. Biol. Chem. (1998) [Pubmed]
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