Please use this identifier to cite or link to this item:
|Title:||Structural insights into small RNA sorting and mRNA target binding by Arabidopsis Argonaute Mid domains|
Adam Yuan, Y.
|Keywords:||5′-End nucleotide specificity loop|
Arabidopsis Argonaute Mid domain
mRNA target binding
Small RNA sorting
|Source:||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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Mar 7, 2018
WEB OF SCIENCETM
checked on Jan 29, 2018
checked on Mar 11, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.