Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA
Models, Molecular
0301 basic medicine
Binding Sites
Base Sequence
Sequence Homology, Amino Acid
Surface Properties
Molecular Sequence Data
Oligonucleotides
Nuclear Proteins
Hydrogen Bonding
DNA
Protein Structure, Secondary
Protein Structure, Tertiary
03 medical and health sciences
Humans
Histone Chaperones
Amino Acid Sequence
Hydrophobic and Hydrophilic Interactions
Conserved Sequence
Histone Acetyltransferases
Protein Binding
DOI:
10.1016/j.jsb.2012.06.014
Publication Date:
2012-07-20T09:25:44Z
AUTHORS (6)
ABSTRACT
Plant homeodomain (PHD) finger is found to be a versatile reader that functions in recruiting transcription factors and chromatin modification complexes. Bromodomain- and PHD finger-containing (BRPF) proteins are identified as scaffold component in a couple of histone acetyltransferase (HATs) complexes but the biological function of PHD fingers, composing the motif called PZPM (PHD/Zn-knuckle/PHD Motif), in BRPF proteins is far from being well understood. Here we report the three-dimensional solution structure of the second PHD finger of PZPM in human BRPF2. According to the structure, BRPF2 PHD2 possesses a two-strand β sheet which is different from any other PHD fingers. Functionally, this PHD finger can potentially bind DNA non-specifically with an evolutionarily conserved and positively charged surface. We provide the structural and interaction information of this atypical PHD finger and categorize this BRPF2 PHD2 into a new subset of PHD finger. Moreover our work also shed light on the functional aspect of the PZPM.
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