Informace o publikaci
New insights into the RISC loading complex
| Autoři | |
|---|---|
| Rok publikování | 2024 |
| Druh | Další prezentace na konferencích |
| Fakulta / Pracoviště MU | |
| Citace | |
| Přiložené soubory | |
| Popis | RNA-silencing pathways rely on small RNAs loaded onto Argonaute proteins to guide sequence-specific transcriptional and post-transcriptional repression of gene expression. Small RNA pathways originating from double-stranded RNA (dsRNA) precursors, such as miRNA and RNAi, require processing by the endonuclease Dicer. Dicer produces a short dsRNA intermediate, from which one strand is selected and loaded onto Argonaute. The molecular mechanisms underlying strand selection are not well understood; however, it is hypothesized that Dicer and/or the HSP70/90 chaperone system facilitate the loading process. Recent advances in electron cryomicroscopy (cryo-EM) have enabled numerous studies of Dicer-RNA complexes, providing previously inaccessible insights into RNA substrate selection and processing by Dicer. However, the structural details of critical events, such as the release of product miRNA and its transfer to Argonaute via the formation of the RISC loading complex, remain elusive. I will summarize the current state of structural analysis of the Dicer-mediated transfer of miRNA to Argonaute and discuss its possible role in the Argonaute loading mechanism. |