Brief Communication abstract
Nature Structural & Molecular Biology 15, 419 - 421 (2008)
Published online: 12 February 2008 | doi:10.1038/nsmb.1400
The ARID domain of the H3K4 demethylase RBP2 binds to a DNA CCGCCC motif
Shengjiang Tu1, Yu-Ching Teng2,3, Chunhua Yuan4, Ying-Ta Wu2, Meng-Yu Chan2, An-Ning Cheng2, Po-Hsun Lin2, Li-Jung Juan2 & Ming-Daw Tsai1,2,4,5
The histone H3 lysine 4 demethylase RBP2 contains a DNA binding domain, the AT-rich interaction domain (ARID). We solved the structure of ARID by NMR, identified its DNA binding motif (CCGCCC) and characterized the binding contacts. Immunofluorescence and luciferase assays indicated that ARID is required for RBP2 demethylase activity in cells and that DNA recognition is essential to regulate transcription.
- Department of Chemistry, Ohio State University, 100 West 18th Ave., Columbus, Ohio 43210, USA.
- Genomics Research Center, Academia Sinica, 128 Academia Rd. Sec. 2, Nankang, Taipei 115, Taiwan.
- Institute of Biochemistry and Molecular Biology, National Yang-Ming University, 115, Sec. 2, Linong St., Beitou, Taipei 112, Taiwan.
- Campus Chemical Instrument Center, 176 West 19th Ave., Ohio State University, Columbus, Ohio 43210, USA.
- Institute of Biological Chemistry, Academia Sinica, 128 Academia Rd., Sec. 2, Nankang, Taipei 115, Taiwan.
Correspondence to: Ming-Daw Tsai1,2,4,5 e-mail: mdtsai@gate.sinica.edu.tw
Correspondence to: Li-Jung Juan2 e-mail: ljjuan@gate.sinica.edu.tw
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