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Toxoplasma gondii parasites uniquely assemble fragmented mitochondrial ribosomal RNAs using nuclear-encoded proteins, including repurposed plant transcription factors. This discovery sheds light on apicomplexan mitoribosome structure and potential therapeutic targets.

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Area of Science:

  • Molecular Biology
  • Parasitology
  • Structural Biology

Background:

  • Apicomplexa are parasites causing significant global disease burden.
  • Their reduced mitochondrial genomes pose challenges in understanding mitoribosome function.
  • Mitoribosomal RNAs (mt-rRNAs) in Apicomplexa are highly fragmented.

Purpose of the Study:

  • To elucidate the assembly and structure of the apicomplexan mitoribosome.
  • To identify the components involved in organizing fragmented mt-rRNAs.
  • To explore the roles of unique RNA-binding proteins in parasite mitochondria.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) for structural analysis.
  • Biochemical assays to study protein-RNA interactions.
  • Genetic analysis of nuclear-encoded mitochondrial proteins.

Main Results:

  • Over 40 mt-rRNA fragments are assembled using nuclear-encoded proteins.
  • Apicetal2/Ethylene Response Factor (AP2/ERF) proteins, originally plant transcription factors, are essential for mitoribosome integrity.
  • Lineage-specific RNA-binding proteins (RAP and HPR families) are crucial components.

Conclusions:

  • Apicomplexan mitoribosomes utilize repurposed transcription factors and novel RNA-binding proteins for assembly.
  • The unique structure highlights parasite-specific adaptations in organellar translation.
  • Understanding these mechanisms may lead to new therapeutic strategies against apicomplexan diseases.