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TitleThe structural basis for RNA slicing by human Argonaute2.
Journal, issue, pagesCell Rep, Vol. 44, Issue 1, Page 115166, Year 2025
Publish dateJan 28, 2025
AuthorsAbdallah A Mohamed / Peter Y Wang / David P Bartel / Seychelle M Vos /
PubMed AbstractArgonaute (AGO) proteins associate with guide RNAs to form complexes that slice transcripts that pair to the guide. This slicing drives post-transcriptional gene silencing through RNA interference ...Argonaute (AGO) proteins associate with guide RNAs to form complexes that slice transcripts that pair to the guide. This slicing drives post-transcriptional gene silencing through RNA interference (RNAi), which is essential for many eukaryotes and the basis for new clinical therapies. Despite this importance, structural information on eukaryotic AGOs in a fully paired, slicing-competent conformation-hypothesized to be intrinsically unstable-has been lacking. Here, we present the cryogenic electron microscopy structure of a human AGO-guide complex bound to a fully paired target, revealing structural rearrangements that enable this conformation. Critically, the N domain of AGO rotates to allow the RNA full access to the central channel and forms contacts that license rapid slicing. Moreover, a conserved loop in the PIWI domain secures the RNA near the active site to enhance slicing rate and specificity. These results explain how AGO accommodates targets possessing pairing specificity typically observed in biological and clinical slicing substrates.
External linksCell Rep / PubMed:39932188 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

45752

9cmp

EMDB-45752, PDB-9cmp:
Structure of human Argonaute2-guide-target complex in a fully paired, slicing-competent conformation
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-45753: The structural basis for RNA slicing by human Argonatue2 (Map 1)
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE/RNA / RNAi / Argonaute / Slicing / HYDROLASE-RNA complex

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