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


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
09 12 2021
Historique:
received: 08 07 2021
accepted: 08 11 2021
entrez: 10 12 2021
pubmed: 11 12 2021
medline: 20 1 2022
Statut: epublish

Résumé

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.

Identifiants

pubmed: 34887394
doi: 10.1038/s41467-021-27200-z
pii: 10.1038/s41467-021-27200-z
pmc: PMC8660880
doi:

Substances chimiques

Mitochondrial Proteins 0
Ribosomal Proteins 0
RNA 63231-63-0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

7176

Informations de copyright

© 2021. The Author(s).

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Auteurs

Florent Waltz (F)

Institut Européen de Chimie et Biologie, U1212 Inserm, Université de Bordeaux, 2 rue R. Escarpit, 33600, Pessac, France.
Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du général Zimmer, 67084, Strasbourg, France.
Helmholtz Pioneer Campus, Helmholtz Zentrum München, Ingolstädter Landstraße 1, 85764, Neuherberg, Germany.

Thalia Salinas-Giegé (T)

Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du général Zimmer, 67084, Strasbourg, France.

Robert Englmeier (R)

Structural Biochemistry, Bijvoet Centre for Biomolecular Research, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands.

Herrade Meichel (H)

Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du général Zimmer, 67084, Strasbourg, France.

Heddy Soufari (H)

Institut Européen de Chimie et Biologie, U1212 Inserm, Université de Bordeaux, 2 rue R. Escarpit, 33600, Pessac, France.

Lauriane Kuhn (L)

Plateforme protéomique Strasbourg Esplanade FRC1589 du CNRS, Université de Strasbourg, 67084, Strasbourg, France.

Stefan Pfeffer (S)

Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany.

Friedrich Förster (F)

Structural Biochemistry, Bijvoet Centre for Biomolecular Research, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands.

Benjamin D Engel (BD)

Helmholtz Pioneer Campus, Helmholtz Zentrum München, Ingolstädter Landstraße 1, 85764, Neuherberg, Germany.
Department of Chemistry, Technical University of Munich, Lichtenbergstraße 4, 85748, Garching, Germany.

Philippe Giegé (P)

Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du général Zimmer, 67084, Strasbourg, France. philippe.giege@ibmp-cnrs.unistra.fr.

Laurence Drouard (L)

Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du général Zimmer, 67084, Strasbourg, France. laurence.drouard@ibmp-cnrs.unistra.fr.

Yaser Hashem (Y)

Institut Européen de Chimie et Biologie, U1212 Inserm, Université de Bordeaux, 2 rue R. Escarpit, 33600, Pessac, France. yaser.hashem@inserm.fr.

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