GTPBP8 plays a role in mitoribosome formation in human mitochondria

Miriam Cipullo, Genís Valentín Gesé, Shreekara Gopalakrishna, Annika Krueger, Vivian Lobo, Maria A. Pirozhkova, James Marks, Petra Páleníková, Dmitrii Shiriaev, Yong Liu, Jelena Misic, Yu Cai, Minh Duc Nguyen, Abubakar Abdelbagi, Xinping Li, Michal Minczuk, Markus Hafner, Daniel Benhalevy, Aishe A. Sarshad, Ilian Atanassov, B. Martin Hällberg and Joanna Rorbach ()
Additional contact information
Miriam Cipullo: Karolinska Institutet
Genís Valentín Gesé: Karolinska Institutet
Shreekara Gopalakrishna: Karolinska Institutet
Annika Krueger: Karolinska Institutet
Vivian Lobo: University of Gothenburg
Maria A. Pirozhkova: Tel Aviv University
James Marks: National Institutes of Health
Petra Páleníková: University of Cambridge
Dmitrii Shiriaev: Karolinska Institutet
Yong Liu: Karolinska Institutet
Jelena Misic: Karolinska Institutet
Yu Cai: Karolinska Institutet
Minh Duc Nguyen: Karolinska Institutet
Abubakar Abdelbagi: Karolinska Institutet
Xinping Li: Max-Planck-Institute for Biology of Ageing
Michal Minczuk: University of Cambridge
Markus Hafner: National Institutes of Health
Daniel Benhalevy: Tel Aviv University
Aishe A. Sarshad: University of Gothenburg
Ilian Atanassov: Max-Planck-Institute for Biology of Ageing
B. Martin Hällberg: Karolinska Institutet
Joanna Rorbach: Karolinska Institutet

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

Abstract: Abstract Mitochondrial gene expression relies on mitoribosomes to translate mitochondrial mRNAs. The biogenesis of mitoribosomes is an intricate process involving multiple assembly factors. Among these factors, GTP-binding proteins (GTPBPs) play important roles. In bacterial systems, numerous GTPBPs are required for ribosome subunit maturation, with EngB being a GTPBP involved in the ribosomal large subunit assembly. In this study, we focus on exploring the function of GTPBP8, the human homolog of EngB. We find that ablation of GTPBP8 leads to the inhibition of mitochondrial translation, resulting in significant impairment of oxidative phosphorylation. Structural analysis of mitoribosomes from GTPBP8 knock-out cells shows the accumulation of mitoribosomal large subunit assembly intermediates that are incapable of forming functional monosomes. Furthermore, fPAR-CLIP analysis reveals that GTPBP8 is an RNA-binding protein that interacts specifically with the mitochondrial ribosome large subunit 16 S rRNA. Our study highlights the role of GTPBP8 as a component of the mitochondrial gene expression machinery involved in mitochondrial large subunit maturation.

Date: 2024
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DOI: 10.1038/s41467-024-50011-x

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