Novel RNA recognition motif domain in the cytoplasmic polyadenylation element binding protein 3

被引：2

作者：

Tsuda, Kengo ^{[1
,2
]}

Kuwasako, Kanako ^{[1
,2
,3
,4
]}

Nagata, Takashi ^{[1
,5
,6
]}

Takahashi, Mari ^{[1
,2
]}

Kigawa, Takanori ^{[1
]}

Kobayashi, Naohiro ^{[1
,7
]}

Guentert, Peter ^{[8
,9
,10
,11
]}

Shirouzu, Mikako ^{[1
,2
]}

Yokoyama, Shigeyuki ^{[1
,12
]}

Muto, Yutaka ^{[1
,2
,3
,4
]}

机构：

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

[2] RIKEN Ctr Life Sci Technol, Div Struct & Synthet Biol, Tsurumi Ku, Yokohama, Kanagawa 2300045, Japan

[3] Musashino Univ, Fac Pharm, Tokyo 2028585, Japan

[4] Musashino Univ, Pharmaceut Sci Res Inst, Tokyo 2028585, Japan

[5] Kyoto Univ, Inst Adv Energy, Struct Energy Biosci Res Sect, Kyoto 6110011, Japan

[6] Kyoto Univ, Grad Sch Energy Sci, Kyoto 6110011, Japan

[7] Osaka Univ, Inst Prot Res, Lab Mol Biophys, Suita, Osaka 5650871, Japan

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

[9] Goethe Univ Frankfurt, Inst Biophys Chem, Ctr Biomol Magnet Resonance, D-60054 Frankfurt, Germany

[10] Goethe Univ Frankfurt, Frankfurt Inst Adv Studies, D-60054 Frankfurt, Germany

[11] Tokyo Metropolitan Univ, Dept Chem, Grad Sch Sci & Engn, Hachioji, Tokyo 19203, Japan

[12] RIKEN Struct Biol Lab, Tsurumi Ku, Yokohama, Kanagawa 2300045, Japan

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2014年 / 82卷 / 10期

基金：

日本学术振兴会;

关键词：

3 '-UTR; CPEB3; CPE; GluR2; Mrna; RRM; NMR; structure; TRANSLATIONAL CONTROL; MESSENGER-RNA; NMR METHODS; DEADENYLASE; DYNAMICS; CPEB3; RRM;

D O I：

10.1002/prot.24651

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 family of cytoplasmic polyadenylation element binding proteins CPEB1, CPEB2, CPEB3, and CPEB4 binds to the 3'-untranslated region (3'-UTR) of mRNA, and plays significant roles in mRNA metabolism and translation regulation. They have a common domain organization, involving two consecutive RNA recognition motif (RRM) domains followed by a zinc finger domain in the C-terminal region. We solved the solution structure of the first RRM domain (RRM1) of human CPEB3, which revealed that CPEB3 RRM1 exhibits structural features distinct from those of the canonical RRM domain. Our structural data provide important information about the RNA binding ability of CPEB3 RRM1. (C) 2014 Wiley Periodicals, Inc.

引用

页码：2879 / 2886

页数：8

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