ArticleScience advances2023
Activation mechanism of a short argonaute-TIR prokaryotic immune system.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Filament assembly induced by the recognition of target DNA activates the prokaryotic Argonaute SPARDA system.Nature communications · 2026Article
- Molecular characterisation of the Bacillus subtilis SpbK antiphage defence system.Nature communications · 2025Article
- Activation of the SPARDA defense system by filament assembly using a beta-relay signaling mechanism widespread in prokaryotic Argonautes.Cell research · 2025Article
- Target DNA-induced filament formation and nuclease activation of SPARDA complex.Cell research · 2025Article
- Structure-guided insights into TIR-mediated bacterial and eukaryotic immunity.Structure (London, England : 1993) · 2025Review
- Structural basis of ssDNA-guided NADase activation of prokaryotic SPARTA system.Nucleic acids research · 2025Article
- Structural and mechanistic insights into the activation of a short prokaryotic argonaute system from archaeon Sulfolobus islandicus.Nucleic acids research · 2025Article
- Mechanistic basis for the allosteric activation of NADase activity in the Sir2-HerA antiphage defense system.Nature communications · 2024Article
- Tetramerization-dependent activation of the Sir2-associated short prokaryotic Argonaute immune system.Nature communications · 2024Article
- Review
- The structural basis of the activation and inhibition of DSR2 NADase by phage proteins.Nature communications · 2024Article
- Nucleic acid mediated activation of a short prokaryotic Argonaute immune system.Nature communications · 2024Article
- Insights into the modulation of bacterial NADase activity by phage proteins.Nature communications · 2024Article
- The missing part: the Archaeoglobus fulgidus Argonaute forms a functional heterodimer with an N-L1-L2 domain protein.Nucleic acids research · 2024Article
- Target DNA-dependent activation mechanism of the prokaryotic immune system SPARTA.Nucleic acids research · 2024Article
- Structural basis of antiphage immunity generated by a prokaryotic Argonaute-associated SPARSA system.Nature communications · 2024Article
- Structures and functions of short argonautes.RNA biology · 2024Review
- Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Short prokaryotic argonaute (pAgo) and toll/interleukin-1 receptor/resistance protein (TIR)-analog of PAZ (APAZ) form a heterodimeric SPARTA complex that provides immunity to its prokaryotic host through an abortive infection mechanism. Monomeric SPARTA senses foreign RNA/DNA duplexes to assemble an active tetramer resulting in cell death by nicotinamide adenine dinucleotide (oxidized form) (NAD) depletion via an unknown mechanism. We report nine structures of SPARTA in different functional states at a resolution range of 4.2 to 2.9 angstroms, revealing its activation mechanism. Inactive SPARTA monomers bind to RNA/DNA duplexes to form symmetric dimers mediated by the association of Ago subunits. The initiation of tetramer assembly induces flexibility of the TIR domains enabling a symmetry-breaking rotational movement of a TIR domain in the dimer units which facilitates the TIR oligomerization, resulting in the formation of the substrate binding pocket and the activation of the SPARTA complex's NADase activity. Our findings provide detailed structural and mechanistic insights into activating a short argonaute defense system.
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