Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation

被引：80

作者：

Jinek, Martin ^{[1
]}

Fabian, Marc R. ^{[2
,3
]}

Coyle, Scott M. ^{[1
,4
]}

Sonenberg, Nahum ^{[2
,3
]}

Doudna, Jennifer A. ^{[1
,4
,5
,6
]}

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] McGill Univ, Dept Biochem, Montreal, PQ, Canada

[3] McGill Univ, Goodman Canc Ctr, Montreal, PQ, Canada

[4] Univ Calif Berkeley, Howard Hughes Med Inst, Berkeley, CA 94720 USA

[5] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[6] Lawrence Berkeley Natl Lab, Phys Biosci Div, Berkeley, CA USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2010年 / 17卷 / 02期

基金：

加拿大健康研究院;

关键词：

POLY(A) BINDING-PROTEIN; TRANSLATIONAL REPRESSION; ARGONAUTE; DOMAIN; COMPLEXES; TNRC6C; CELLS; PAIP2;

D O I：

10.1038/nsmb.1768

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：

GW182-family proteins are essential for microRNA-mediated translational repression and deadenylation in animal cells. Here we show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex. Mutations at the complex interface impair mRNA deadenylation in mammalian cell extracts, suggesting that the GW182-PABC interaction contributes to microRNA-mediated gene silencing.

引用

页码：238 / 240

页数：3

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