Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA

• DOI: 10.1016/j.jsb.2012.06.014
• Publication Date: 2012-07-20T09:25:44Z
• Authors: Lei Liu; Su Qin; Jiahai Zhang; Peng Ji; Yunyu Shi; Jihui Wu
• Keywords: 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

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.