WestminsterResearch

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

Chen, Dongsheng and Lucey, Marie J. and Phoenix, Fladia and Lopez-Garcia, Jorge and Hart, Stephen M. and Losson, Regine and Buluwela, Lakjaya and Coombes, R. Charles and Chambon, Pierre and Schar, Primo and Ali, Simak (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. ISSN 0021-9258

Full text not available from this repository.

Official URL: http://dx.doi.org/10.1074/jbc.M304286200

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.

Item Type:Article
Additional Information:Online ISSN 1083-351X
Research Community:University of Westminster > Life Sciences, School of
ID Code:3557
Deposited On:27 Feb 2007
Last Modified:10 Apr 2008 14:13

Repository Staff Only: item control page