Structural Insight into the Zinc Finger CW Domain as a Histone Modification Reader

被引：89

作者：

He, Fahu ^{[1
]}

Umehara, Takashi ^{[1
]}

Saito, Kohei ^{[1
]}

Harada, Takushi ^{[1
]}

Watanabe, Satoru ^{[1
]}

Yabuki, Takashi ^{[1
]}

Kigawa, Takanori ^{[1
,2
]}

Takahashi, Mari ^{[1
]}

Kuwasako, Kanako ^{[1
]}

Tsuda, Kengo ^{[1
]}

Matsuda, Takayoshi ^{[1
]}

Aoki, Masaaki ^{[1
]}

Seki, Eiko ^{[1
]}

Kobayashi, Naohiro ^{[1
]}

Guentert, Peter ^{[3
,4
,5
]}

Yokoyama, Shigeyuki ^{[1
,6
]}

Muto, Yutaka ^{[1
]}

机构：

[1] RIKEN Syst & Struct Biol Ctr, Tsurumi Ku, Yokohama, Kanagawa 2300045, Japan

[2] Tokyo Inst Technol, Midori Ku, Yokohama, Kanagawa 2268502, Japan

[3] RIKEN Genom Sci Ctr, Tatsuo Miyazawa Mem Program, Yokohama, Kanagawa 2300045, Japan

[4] Goethe Univ Frankfurt, Frankfurt Inst Adv Studies, D-60438 Frankfurt, Germany

[5] Goethe Univ Frankfurt, Inst Biophys Chem, Ctr Biomol Magnet Resonance, D-60438 Frankfurt, Germany

[6] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Bunkyo Ku, Tokyo 1130033, Japan

来源：

STRUCTURE | 2010年 / 18卷 / 09期

基金：

日本学术振兴会;

关键词：

PHD FINGER; NMR STRUCTURE; METHYLATION; PROTEIN; RECOGNITION; ARABIDOPSIS; DEMETHYLASE; DYNAMICS; PROGRAMS; H3K4ME3;

D O I：

10.1016/j.str.2010.06.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1127 / 1139

页数：13

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