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| Title | Structural basis of microRNA processing by Dicer-like 1. |
|---|---|
| Journal, issue, pages | Nat Plants, Vol. 7, Issue 10, Page 1389-1396, Year 2021 |
| Publish date | Sep 30, 2021 |
 Authors | Xiaobin Wei / Huanhuan Ke / Aijia Wen / Bo Gao / Jing Shi / Yu Feng /  |
| PubMed Abstract | MicroRNAs (miRNAs) are short non-coding RNAs that inhibit the expression of target genes by directly binding to their mRNAs. In animals, pri-miRNAs are cleaved by Drosha to generate pre-miRNAs, which ...MicroRNAs (miRNAs) are short non-coding RNAs that inhibit the expression of target genes by directly binding to their mRNAs. In animals, pri-miRNAs are cleaved by Drosha to generate pre-miRNAs, which are subsequently cleaved by Dicer to generate mature miRNAs. Instead of being cleaved by two different enzymes, both cleavages in plants are performed by Dicer-like 1 (DCL1). With a similar domain architecture as human Dicer, it is mysterious how DCL1 recognizes pri-miRNAs and performs two cleavages sequentially. Here, we report the single-particle cryo-electron microscopy structures of Arabidopsis DCL1 complexed with a pri-miRNA and a pre-miRNA, respectively, in cleavage-competent states. These structures uncover the plasticity of the PAZ domain, which is critical for the recognition of both pri-miRNA and pre-miRNA. These structures suggest that the helicase module serves as an engine that transfers the substrate between two sequential cleavage events. This study lays a foundation for dissecting the regulation mechanism of miRNA biogenesis in plants and provides insights into the dicing state of human Dicer. |
 External links | Nat Plants / PubMed:34593993 |
| Methods | EM (single particle) |
| Resolution | 4.6 - 4.9 Å |
| Structure data | EMDB-31181, PDB-7eld: EMDB-31182, PDB-7ele: |
| Source |
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 Keywords |  HYDROLASE / MicroRNA / miRNA / Endonuclease / Helicase / Nuclease / RNA-binding |
