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Scaltsoyiannes, V.* ; Corre, N.* ; Waltz, F. ; Giegé, P.*

Types and functions of mitoribosome-specific ribosomal proteins across eukaryotes.

Int. J. Mol. Sci. 23:3474 (2022)
Publ. Version/Full Text DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
Mitochondria are key organelles that combine features inherited from their bacterial endosymbiotic ancestor with traits that arose during eukaryote evolution. These energy producing organelles have retained a genome and fully functional gene expression machineries including specific ribosomes. Recent advances in cryo-electron microscopy have enabled the characterization of a fast-growing number of the low abundant membrane-bound mitochondrial ribosomes. Surprisingly, mitoribosomes were found to be extremely diverse both in terms of structure and composition. Still, all of them drastically increased their number of ribosomal proteins. Interestingly, among the more than 130 novel ribosomal proteins identified to date in mitochondria, most of them are composed of a-helices. Many of them belong to the nuclear encoded super family of helical repeat proteins. Here we review the diversity of functions and the mode of action held by the novel mitoribosome proteins and discuss why these proteins that share similar helical folds were independently recruited by mitoribosomes during evolution in independent eukaryote clades.
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Publication type Article: Journal article
Document type Review
Corresponding Author
Keywords Helical Repeat Proteins ; Mitochondrial Gene Expression ; Pentatricopeptide Repeat Proteins ; Ribosomes ; Single Particle Cryo-em ; Translation
ISSN (print) / ISBN 1422-0067
e-ISSN 1661-6596
Quellenangaben Volume: 23, Issue: 7, Pages: , Article Number: 3474 Supplement: ,
Publisher MDPI
Publishing Place Basel
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Helmholtz Pioneer Campus (HPC)
Grants Agence Nationale de la Recherche