Crystal structure of zinc-finger domain of Nanos and its functional implications

被引：29

作者：

Hashimoto, Hiroshi ^{[1
]}

Hara, Kodai ^{[1
]}

Hishiki, Asami ^{[1
]}

Kawaguchi, Shigeta ^{[1
]}

Shichijo, Naoki ^{[1
]}

Nakamura, Keishi ^{[2
]}

Unzai, Satoru ^{[1
]}

Tamaru, Yutaka ^{[2
]}

Shimizu, Toshiyuki ^{[3
]}

Sato, Mamoru ^{[1
]}

机构：

[1] Yokohama City Univ, Grad Sch Nanobiosci, Tsurumi Ku, Kanagawa 2300045, Japan

[2] Mie Univ, Grad Sch Bioresources, Tsu, Mie 5148507, Japan

[3] Univ Tokyo, Grad Sch Pharmaceut Sci, Bunkyo Ku, Tokyo 1130033, Japan

来源：

EMBO REPORTS | 2010年 / 11卷 / 11期

关键词：

crystal structure; germ cell; Nanos; RNA-binding protein; translational regulation; GERMLINE STEM-CELLS; DNA-BINDING DOMAIN; X-RAY-DIFFRACTION; MESSENGER-RNA; TRANSLATIONAL CONTROL; NUCLEOCAPSID PROTEIN; DROSOPHILA EMBRYOS; ZEBRAFISH NANOS; PUMILIO; RECOGNITION;

D O I：

10.1038/embor.2010.155

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：

Nanos is an RNA-binding protein that is involved in the development and maintenance of germ cells. In combination with Pumilio, Nanos binds to the 3' untranslated region of a messenger RNA and represses its translation. Nanos has two conserved Cys-Cys-His-Cys zinc-finger motifs that are indispensable for its function. In this study, we have determined the crystal structure of the zinc-finger domain of zebrafish Nanos, for the first time revealing that Nanos adopts a novel zinc-finger structure. In addition, Nanos has a conserved basic surface that is directly involved in RNA binding. Our results provide the structural basis for further studies to clarify Nanos function.

引用

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页码：848 / 853

页数：6

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