ArticleNucleic acids research2024
Target DNA-dependent activation mechanism of the prokaryotic immune system SPARTA.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Structural insights into C-terminus-mediated RNA target cleavage by a mesophilic prokaryotic argonaute.Nature communications · 2026Article
- Activation of the SPARDA defense system by filament assembly using a beta-relay signaling mechanism widespread in prokaryotic Argonautes.Cell research · 2025Article
- Argonaute-HNH filaments triggered by invader DNA confer bacterial immunity.Nature communications · 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
- Nucleic acid mediated activation of a short prokaryotic Argonaute immune system.Nature communications · 2024Article
- DNA-targeting short Argonautes complex with effector proteins for collateral nuclease activity and bacterial population immunity.Nature microbiology · 2024Article
- Insights into the modulation of bacterial NADase activity by phage proteins.Nature communications · 2024Article
- Structures and functions of short argonautes.RNA biology · 2024Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
In both prokaryotic and eukaryotic innate immune systems, TIR domains function as NADases that degrade the key metabolite NAD+ or generate signaling molecules. Catalytic activation of TIR domains requires oligomerization, but how this is achieved varies in distinct immune systems. In the Short prokaryotic Argonaute (pAgo)/TIR-APAZ (SPARTA) immune system, TIR NADase activity is triggered upon guide RNA-mediated recognition of invading DNA by an unknown mechanism. Here, we describe cryo-EM structures of SPARTA in the inactive monomeric and target DNA-activated tetrameric states. The monomeric SPARTA structure reveals that in the absence of target DNA, a C-terminal tail of TIR-APAZ occupies the nucleic acid binding cleft formed by the pAgo and TIR-APAZ subunits, inhibiting SPARTA activation. In the active tetrameric SPARTA complex, guide RNA-mediated target DNA binding displaces the C-terminal tail and induces conformational changes in pAgo that facilitate SPARTA-SPARTA dimerization. Concurrent release and rotation of one TIR domain allow it to form a composite NADase catalytic site with the other TIR domain within the dimer, and generate a self-complementary interface that mediates cooperative tetramerization. Combined, this study provides critical insights into the structural architecture of SPARTA and the molecular mechanism underlying target DNA-dependent oligomerization and catalytic activation.
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