How to build a ribosome from RNA fragments in Chlamydomonas mitochondria

Florent Waltz, Thalia Salinas-Giegé, Robert Englmeier, Herrade Meichel, Heddy Soufari, Lauriane Kuhn, Stefan Pfeffer, Friedrich Förster, Benjamin D. Engel, Philippe Giegé (), Laurence Drouard () and Yaser Hashem ()
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Florent Waltz: Université de Bordeaux
Thalia Salinas-Giegé: Université de Strasbourg
Robert Englmeier: Utrecht University
Herrade Meichel: Université de Strasbourg
Heddy Soufari: Université de Bordeaux
Lauriane Kuhn: Université de Strasbourg
Stefan Pfeffer: Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance
Friedrich Förster: Utrecht University
Benjamin D. Engel: Helmholtz Zentrum München
Philippe Giegé: Université de Strasbourg
Laurence Drouard: Université de Strasbourg
Yaser Hashem: Université de Bordeaux

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract Mitochondria are the powerhouse of eukaryotic cells. They possess their own gene expression machineries where highly divergent and specialized ribosomes, named hereafter mitoribosomes, translate the few essential messenger RNAs still encoded by mitochondrial genomes. Here, we present a biochemical and structural characterization of the mitoribosome in the model green alga Chlamydomonas reinhardtii, as well as a functional study of some of its specific components. Single particle cryo-electron microscopy resolves how the Chlamydomonas mitoribosome is assembled from 13 rRNA fragments encoded by separate non-contiguous gene pieces. Additional proteins, mainly OPR, PPR and mTERF helical repeat proteins, are found in Chlamydomonas mitoribosome, revealing the structure of an OPR protein in complex with its RNA binding partner. Targeted amiRNA silencing indicates that these ribosomal proteins are required for mitoribosome integrity. Finally, we use cryo-electron tomography to show that Chlamydomonas mitoribosomes are attached to the inner mitochondrial membrane via two contact points mediated by Chlamydomonas-specific proteins. Our study expands our understanding of mitoribosome diversity and the various strategies these specialized molecular machines adopt for membrane tethering.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27200-z

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DOI: 10.1038/s41467-021-27200-z

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