Structural insights into small RNA sorting and mRNA target binding by Arabidopsis Argonaute Mid domains |
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Authors: | Xingfu Zha Qingyou Xia Y Adam Yuan |
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Affiliation: | a Department of Biological Sciences and Centre for Bioimaging Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore b State Key Laboratory of Silkworm Genome Biology, College of Biotechnology, Southwest University, Beibei, Chongqing 400715, China c Temasek Life Sciences Laboratory, National University of Singapore, 1 Research Link, Singapore 117604, Singapore |
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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. |
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Keywords: | Crystal structure Arabidopsis Argonaute Mid domain 5&prime -End nucleotide specificity loop Small RNA sorting mRNA target binding |
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