The ARID domain of the H3K4 demethylase RBP2 binds to a DNA CCGCCC motif
Author(s) -
Shengjiang Tu,
YuChing Teng,
Yuan Chun-hua,
YingTa Wu,
Meng-Yu Chan,
AnNing Cheng,
PoHsun Lin,
LiJung Juan,
MingDaw Tsai
Publication year - 2008
Publication title -
nature structural and molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.448
H-Index - 270
eISSN - 1545-9993
pISSN - 1545-9985
DOI - 10.1038/nsmb.1400
Subject(s) - demethylase , histone , dna , chemistry , microbiology and biotechnology , hmg box , sequence motif , biochemistry , transcription factor , biology , dna binding protein , gene
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom