Apicomplexan mitoribosome from highly fragmented rRNAs to a functional machine

Chaoyue Wang, Sari Kassem, Rafael Eduardo Oliveira Rocha, Pei Sun, Tan-Trung Nguyen, Joachim Kloehn, Xianyong Liu, Lorenzo Brusini, Alessandro Bonavoglia, Sramona Barua, Fanny Boissier, Mayara Lucia Del Cistia, Hongjuan Peng, Xinming Tang, Fujie Xie, Zixuan Wang, Oscar Vadas, Xun Suo (), Yaser Hashem (), Dominique Soldati-Favre () and Yonggen Jia ()
Additional contact information
Chaoyue Wang: China Agricultural University
Sari Kassem: University of Geneva
Rafael Eduardo Oliveira Rocha: Université de Bordeaux
Pei Sun: Guangdong Academy of Science
Tan-Trung Nguyen: Université de Bordeaux
Joachim Kloehn: University of Geneva
Xianyong Liu: China Agricultural University
Lorenzo Brusini: University of Geneva
Alessandro Bonavoglia: University of Geneva
Sramona Barua: Université de Bordeaux
Fanny Boissier: Université de Bordeaux
Mayara Lucia Del Cistia: Université de Bordeaux
Hongjuan Peng: Southern Medical University
Xinming Tang: Chinese Academy of Agricultural Sciences
Fujie Xie: China Agricultural University
Zixuan Wang: China Agricultural University
Oscar Vadas: University of Geneva
Xun Suo: China Agricultural University
Yaser Hashem: Université de Bordeaux
Dominique Soldati-Favre: University of Geneva
Yonggen Jia: Capital Medical University

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract The phylum Apicomplexa comprises eukaryotic parasites that cause fatal diseases affecting millions of people and animals worldwide. Their mitochondrial genomes have been significantly reduced, leaving only three protein-coding genes and highly fragmented mitoribosomal rRNAs, raising challenging questions about mitoribosome composition, assembly and structure. Our study reveals how Toxoplasma gondii assembles over 40 mt-rRNA fragments using exclusively nuclear-encoded mitoribosomal proteins and three lineage-specific families of RNA-binding proteins. Among these are four proteins from the Apetala2/Ethylene Response Factor (AP2/ERF) family, originally known as transcription factors in plants and Apicomplexa, now repurposed as essential mitoribosome components. Cryo-EM analysis of the mitoribosome structure demonstrates how these AP2 proteins function as RNA binders to maintain mitoribosome integrity. The mitoribosome is also decorated with members of lineage-specific RNA-binding proteins belonging to RAP (RNA-binding domain abundant in Apicomplexa) proteins and HPR (heptatricopeptide repeat) families, highlighting the unique adaptations of these parasites. Solving the molecular puzzle of apicomplexan mitoribosome could inform the development of therapeutic strategies targeting organellar translation.

Date: 2024
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DOI: 10.1038/s41467-024-55033-z

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