Arabidopsis Argonaute MID domains use their nucleotide specificity loop to sort small RNAs

被引：74

作者：

Frank, Filipp ^{[1
,2
,3
]}

Hauver, Jesse ^{[1
]}

Sonenberg, Nahum ^{[1
,3
]}

Nagar, Bhushan ^{[1
,2
]}

机构：

[1] McGill Univ, Dept Biochem, Montreal, PQ H3G 0B1, Canada

[2] McGill Univ, Grp Rech Axe Struct Prot, Montreal, PQ, Canada

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

来源：

EMBO JOURNAL | 2012年 / 31卷 / 17期

基金：

加拿大健康研究院; 加拿大自然科学与工程研究理事会;

关键词：

Argonaute MID domains; Argonaute sorting; crystallography; NMR; small RNAs; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; MESSENGER-RNA; ENDOGENOUS SIRNAS; GUIDE RNA; RECOGNITION; BINDING; SOFTWARE; INSIGHTS; REVEALS;

D O I：

10.1038/emboj.2012.204

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 5'-nucleotide of small RNAs associates directly with the MID domain of Argonaute (AGO) proteins. In humans, the identity of the 5'-base is sensed by the MID domain nucleotide specificity loop and regulates the integrity of miRNAs. In Arabidopsis thaliana, the 5'-nucleotide also controls sorting of small RNAs into the appropriate member of the AGO family; however, the structural basis for this mechanism is unknown. Here, we present crystal structures of the MID domain from three Arabidopsis AGOs, AtAGO1, AtAGO2 and AtAGO5, and characterize their interactions with nucleoside monophosphates (NMPs). In AtAGOs, the nucleotide specificity loop also senses the identity of the 5'-nucleotide but uses more diverse modes of recognition owing to the greater complexity of small RNAs found in plants. Binding analyses of these interactions reveal a strong correlation between their affinities and evolutionary conservation. The EMBO Journal (2012) 31, 3588-3595. doi:10.1038/emboj.2012.204; Published online 31 July 2012 Subject Categories: RNA; plant biology

引用

页码：3588 / 3595

页数：8

共 44 条

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