Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.febslet.2012.06.038
Title: Structural insights into small RNA sorting and mRNA target binding by Arabidopsis Argonaute Mid domains
Authors: Zha, X.
Xia, Q.
Adam Yuan, Y. 
Keywords: 5′-End nucleotide specificity loop
Arabidopsis Argonaute Mid domain
Crystal structure
mRNA target binding
Small RNA sorting
Issue Date: 21-Sep-2012
Citation: Zha, X., Xia, Q., Adam Yuan, Y. (2012-09-21). Structural insights into small RNA sorting and mRNA target binding by Arabidopsis Argonaute Mid domains. FEBS Letters 586 (19) : 3200-3207. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2012.06.038
Abstract: The RISC-associated Argonaute (Ago) proteins play the catalytic role for RISC-mediated gene regulation by selecting small RNAs and subsequent targeting and cleavage of complementary mRNAs. Ago Mid domains are proposed to play essential roles in small RNA sorting. Here, we report the crystal structures of Arabidopsis Ago1 Mid domain and its chimera mutant with part of Ago1 replaced by Ago4. The structures demonstrate that a single amino insertion in the nucleotide specificity loop of AtAgo1 will change the nucleotide binding preference of AtAgo1 from "5′-U" to "5′-A". Moreover, we identify a long positively charged groove located along the "5′-end-nucleotide specificity loop" and occupied by several sulfate ions with the distance of 9-11 Å distance, indicating a putative mRNA target binding groove. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Source Title: FEBS Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/101763
ISSN: 00145793
DOI: 10.1016/j.febslet.2012.06.038
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