Structural insight into the zinc finger CW domain as a histone modification reader.
The zinc finger CW (zf-CW) domain is a motif of about 60 residues that is frequently found in proteins involved in epigenetic regulation. Here, we determined the NMR solution structure of the zf-CW domain of the human zf-CW and PWWP domain containing protein 1 (ZCWPW1). The zf-CW domain adopts a new fold in which a zinc ion is coordinated tetrahedrally by four conserved Cys ligand residues. The tertiary structure of the zf-CW domain partially resembles that adopted by the plant homeo domain (PHD) finger bound to the histone tail, suggesting that the zf-CW domain and the PHD finger have similar functions. The solution structure of the complex of the zf-CW domain with the histone H3 tail peptide (1-10) with trimethylated K4 clarified its binding mode. Our structural and biochemical studies have identified the zf-CW domain as a member of the histone modification reader modules for epigenetic regulation.
He
Fahu
F
RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Umehara
Takashi
T
Saito
Kohei
K
Harada
Takushi
T
Watanabe
Satoru
S
Yabuki
Takashi
T
Kigawa
Takanori
T
Takahashi
Mari
M
Kuwasako
Kanako
K
Tsuda
Kengo
K
Matsuda
Takayoshi
T
Aoki
Masaaki
M
Seki
Eiko
E
Kobayashi
Naohiro
N
Güntert
Peter
P
Yokoyama
Shigeyuki
S
Muto
Yutaka
Y
D000595:Amino Acid Sequence; D001665:Binding Sites; D044127:Epigenesis, Genetic; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D016335:Zinc Fingers
D006657:Histones