Abstract
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.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
DNA / metabolism*
-
Fluorescent Antibody Technique
-
Humans
-
Nuclear Magnetic Resonance, Biomolecular
-
Promoter Regions, Genetic
-
Protein Binding
-
Protein Serine-Threonine Kinases / genetics
-
Retinol-Binding Proteins, Cellular / chemistry
-
Retinol-Binding Proteins, Cellular / metabolism*
-
Structure-Activity Relationship
-
Transcription Factors
Substances
-
BRD2 protein, human
-
RBP2 protein, human
-
Retinol-Binding Proteins, Cellular
-
Transcription Factors
-
DNA
-
Protein Serine-Threonine Kinases