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TitleTarget DNA-induced filament formation and nuclease activation of SPARDA complex.
Journal, issue, pagesCell Res, Vol. 35, Issue 7, Page 510-519, Year 2025
Publish dateMar 24, 2025
AuthorsFeng Wang / Haijiang Xu / Chendi Zhang / Jialin Xue / Zhuang Li /
PubMed AbstractThe short Argonaute-based bacterial defense system, SPARDA (Short Prokaryotic Argonaute and DNase/RNase-APAZ), utilizes guide RNA to target invading complementary DNA and exhibits collateral nuclease ...The short Argonaute-based bacterial defense system, SPARDA (Short Prokaryotic Argonaute and DNase/RNase-APAZ), utilizes guide RNA to target invading complementary DNA and exhibits collateral nuclease activity, leading to cell death or dormancy. However, its detailed mechanisms remain poorly understood. In this study, we investigated the SPARDA system from Novosphingopyxis baekryungensis (NbaSPARDA) and discovered an unexpected filament configuration upon target DNA binding, which strongly correlated with collateral nuclease activity. Filament formation and nuclease activation require a guide-target heteroduplex of sufficient length with perfect complementarity at the central region. A series of cryo-EM structures of NbaSPARDA complexes, loaded with guide RNA, target DNA of varying lengths, and substrate ssDNA, were determined at ~3.0 Å resolution. Structural analyses indicated that guide RNA binding induces dimerization of the NbaSPARDA complex, while target DNA engagement disrupts this dimerization. Further propagation of the guide-target heteroduplex triggers filament formation through a checkpoint mechanism. The NbaSPARDA filament consists of a backbone formed by interlocking short Argonaute proteins, with an inner layer composed of DREN nuclease domains. Filament formation leads to tetramerization of the monomeric DREN nuclease domain, activating its collateral nuclease activity against environmental nucleic acids - a feature leveraged for molecular diagnostics. For bacteria heterologously expressing the NbaSPARDA system, defense against invading bacteriophages and plasmids relies on filament formation. Collectively, these findings illustrate the detailed working mechanism of the NbaSPARDA complex and highlight the importance of its filament formation in host defense.
External linksCell Res / PubMed:40122999 / PubMed Central
MethodsEM (single particle)
Resolution2.93 - 3.34 Å
Structure data

61769

9jsb

EMDB-61769, PDB-9jsb:
guide-bound NbaSPARDA complexes
Method: EM (single particle) / Resolution: 2.93 Å

61780

9jsp

EMDB-61780, PDB-9jsp:
inactive NbaSPARDA complexes
Method: EM (single particle) / Resolution: 3.34 Å

61787

9jsz

EMDB-61787, PDB-9jsz:
active NbaSPARDA complexes
Method: EM (single particle) / Resolution: 3.18 Å

61790

9jt2

EMDB-61790, PDB-9jt2:
substrate-bound NbaSPARDA complexes
Method: EM (single particle) / Resolution: 3.19 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • novosphingopyxis baekryungensis dsm 16222 (bacteria)
KeywordsRNA BINDING PROTEIN/RNA / protein / RNA / RNA BINDING PROTEIN-RNA complex / RNA BINDING PROTEIN/RNA/DNA / DNA / RNA BINDING PROTEIN-RNA-DNA complex / RNA BINDING PROTEIN

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