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Salinas-Giegé, T.* ; Englmeier, R.* ; Meichel, H.* ; Soufari, H.* ; Kühn, L.* ; Pfeffer, S.* ; Förster, F.* ; Engel, B.D. ; Giegé, P.* ; Drouard, L.* ; Hashem, Y.* ; Waltz, F.

How to build a ribosome from RNA fragments in Chlamydomonas mitochondria.

Nat. Commun. 12:7176 (2021)
Publ. Version/Full Text DOI PMC
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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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Respiratory-deficient Mutants; Green-alga Chlamydomonas; P-32 Protein; In-situ; Subunit; Gene; Reinhardtii; Mutations; Identification; Visualization
Language english
Publication Year 2021
HGF-reported in Year 2021
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Journal Nature Communications
Quellenangaben Volume: 12, Issue: 1, Pages: , Article Number: 7176 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Helmholtz Pioneer Campus (HPC)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Pioneer Campus
PSP Element(s) G-510008-001
Grants Agence Nationale de la Recherche (French National Research Agency)
DOI 10.1038/s41467-021-27200-z
WOS ID WOS:000728562700013
Scopus ID 85121004435
PubMed ID 34887394
Erfassungsdatum 2021-12-21
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