The ARID domain of the H3K4 demethylase RBP2 binds to a DNA CCGCCC motif.
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.
Tu
Shengjiang
S
Department of Chemistry, Ohio State University, 100 West 18th Ave., Columbus, Ohio 43210, USA.
Teng
Yu-Ching
YC
Yuan
Chunhua
C
Wu
Ying-Ta
YT
Chan
Meng-Yu
MY
Cheng
An-Ning
AN
Lin
Po-Hsun
PH
Juan
Li-Jung
LJ
Tsai
Ming-Daw
MD
D004247:DNA / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000235:genetics; D054840:Retinol-Binding Proteins, Cellular / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014157:Transcription Factors; D000092468:Bromodomain Containing Proteins
D004247:DNA; D017346:Protein Serine-Threonine Kinases; D054840:Retinol-Binding Proteins, Cellular; D014157:Transcription Factors; C098415:BRD2 protein, human; D000092468:Bromodomain Containing Proteins; C518459:RBP2 protein, human