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Structural and functional characterization of SPARTA system.

Hongze Zhao1, Pingping Huang2, Lijie Guo1

  • 1State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing, 210009, China; Department of Pharmacology, School of Pharmacy, China Pharmaceutical University, Nanjing, 210009, China.

Biochemical and Biophysical Research Communications
|May 22, 2026
PubMed
Summary
This summary is machine-generated.

Bacterial SPARTA (Short prokaryotic Argonaute associated with TIR-APAZ) systems show activity differences due to TIR domain flexibility. This flexibility, influenced by temperature and Ca2+, impacts NAD+ depletion and suggests tRNA fragments as guide RNAs.

Keywords:
AgonauteDefense systemGuide RNASPARTAtRNA

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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Short prokaryotic Argonaute associated with TIR-APAZ (SPARTA) is a bacterial defense system.
  • SPARTA oligomerizes to activate its TIR domain, depleting NAD+ upon target DNA recognition.
  • Activity divergence exists between thermophilic Crenotalea thermophila SPARTA (CrtSPARTA) and Maribacter polysiphoniae SPARTA (MapSPARTA).

Purpose of the Study:

  • To elucidate the mechanism behind the activity divergence between CrtSPARTA and MapSPARTA.
  • To investigate the role of flexibility and domain interactions in SPARTA activation.
  • To identify potential guide RNAs and cooperative mechanisms for SPARTA function.

Main Methods:

  • Biochemical analysis
  • Structural analysis
  • Site-directed mutagenesis

Main Results:

  • MapSPARTA exhibits greater TIR domain flexibility compared to the rigid CrtSPARTA, with TIR domain flipping during tetramer formation.
  • Weakening the MID-TIR interaction enhanced CrtSPARTA activity, suggesting this interaction restricts activation.
  • Higher temperatures and Ca2+ promote flexibility-induced activation of MapSPARTA, while CrtSPARTA's activation is restricted.
  • tRNA fragments were identified as potential guide RNAs for SPARTA activation.

Conclusions:

  • The MID-TIR interaction acts as a regulatory mechanism to prevent auto-activation of thermophilic CrtSPARTA.
  • Flexibility of the TIR domain is a key determinant of SPARTA activity and regulation.
  • SPARTA may cooperate with tRNA endonucleases, utilizing tRNA fragments as guides for enhanced defense against viral infections.