T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor α

Chen, D., Lucey, M.J., Phoenix, F., Lopez-Garcia, J., Hart, S.M., Losson, R., Buluwela, L., Coombes, R.C., Chambon, P., Schar, P. and Ali, S. 2003. T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor α. Journal of Biological Chemistry. 278 (40), pp. 38586-38592. https://doi.org/10.1074/jbc.M304286200

TitleT:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor α
AuthorsChen, D., Lucey, M.J., Phoenix, F., Lopez-Garcia, J., Hart, S.M., Losson, R., Buluwela, L., Coombes, R.C., Chambon, P., Schar, P. and Ali, S.
Abstract

Nuclear receptors (NR) classically regulate gene expression by stimulating transcription upon binding to their cognate ligands. It is now well established that NR-mediated transcriptional activation requires the recruitment of coregulator complexes, which facilitate recruitment of the basal transcription machinery through direct interactions with the basal transcription machinery and/or through chromatin remodeling. However, a number of recently described NR coactivators have been implicated in cross-talk with other nuclear processes including RNA splicing and DNA repair. T:G mismatch-specific thymine DNA glycosylase (TDG) is required for base excision repair of deaminated methylcytosine. Here we show that TDG is a coactivator for estrogen receptor (ER). We demonstrate that TDG interacts with ER in vitro and in vivo and suggest a separate role for TDG to its established role in DNA repair. We show that this involves helix 12 of ER. The region of interaction in TDG is mapped to a putative -helical motif containing a motif distinct from but similar to the LXXLL motif that mediates interaction with NR. Together with recent reports linking TFIIH in regulating NR function, our findings provide new data to further support an important link between DNA repair proteins and nuclear receptor function.

JournalJournal of Biological Chemistry
Journal citation278 (40), pp. 38586-38592
ISSN0021-9258
YearOct 2003
Digital Object Identifier (DOI)https://doi.org/10.1074/jbc.M304286200
Publication dates
PublishedOct 2003

Related outputs

T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif
Lucey, M.J., Chen, D., Lopez-Garcia, J., Hart, S.M., Phoenix, F., Al-Jehani, R., Alao, J.P., White, R., Kindle, K.B., Losson, R., Chambon, P., Parker, M.G., Schar, P., Heery, D.M., Buluwela, L. and Ali, S. 2005. T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif. Nucleic Acids Research. 33 (19), pp. 6393-6404. https://doi.org/10.1093/nar/gki940

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