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
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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