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DNA Damage and Cellular Stress Responses

E2FBP1/DRIL1, an AT-Rich Interaction Domain-Family Transcription Factor, Is Regulated by p53¹

¹ Section of Molecular Embryology, Graduate School and ² Department of Biochemical Genetics, Medical Research Institute, Tokyo Medical and Dental University, Yushima, Bunkyo-ku, Tokyo, Japan

Requests for reprints: Masa-Aki Ikeda, Section of Molecular Embryology, Graduate School, Tokyo Medical and Dental University, 1-5-45, Yushima, Bunkyo-ku, Tokyo 113-8549, Japan. Phone: 81-3-5803-5579; Fax: 81-3-5803-0213. E-mail: mikeda.emb{at}tmd.ac.jp

E2FBP1/DRIL1 is an AT-rich interaction domain DNA-binding protein and is ubiquitously expressed in various tissues. It has been shown that Bright, the mouse orthologue of E2FBP1/DRIL1, exhibits sequence-specific DNA binding and regulates immunoglobulin transcription. Here we show a novel connection between E2FBP1/DRIL1 and the p53 tumor suppressor, a key regulator of growth arrest or apoptosis in response to cellular stress. We found a putative p53-binding site, which specifically responded to p53, in the second intron of the E2FBP1/DRIL1 gene. E2FBP1/DRIL1was induced by p53 and up-regulated following DNA damage caused by UV radiation or doxorubicin treatment in a manner dependent on endogenous p53. The ectopic expression of E2FBP1/DRIL1 induced growth arrest in U2OS cells expressing normal p53, but not Saos-2 cells lacking p53. These results suggest that E2FBP1/DRIL1 may play a role in growth suppression mediated by p53.

Key Words: p53 • gene expression • E2FBP1 • DRIL1 • ARID • Bright

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