Structural Insights into the Mechanism of Mitoribosomal Large Subunit Biogenesis.
Cryoelectron Microscopy
DEAD-box RNA Helicases
/ chemistry
GTP Phosphohydrolases
/ chemistry
Mitochondrial Ribosomes
/ chemistry
Models, Molecular
Nucleic Acid Conformation
RNA, Ribosomal
/ chemistry
Ribosomal Proteins
/ chemistry
Ribosome Subunits, Large
/ chemistry
Trypanosoma brucei brucei
/ genetics
Trypanosoma brucei
assembly factors
cryo-EM structure
mitochondrial ribosome
mitoribosome
peptidyltransferase center
ribosomal GTPases
ribosomal maturation
ribosome assembly
ribosome biogenesis
Journal
Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571
Informations de publication
Date de publication:
20 08 2020
20 08 2020
Historique:
received:
27
02
2020
revised:
04
05
2020
accepted:
11
06
2020
pubmed:
18
7
2020
medline:
25
9
2020
entrez:
18
7
2020
Statut:
ppublish
Résumé
In contrast to the bacterial translation machinery, mitoribosomes and mitochondrial translation factors are highly divergent in terms of composition and architecture. There is increasing evidence that the biogenesis of mitoribosomes is an intricate pathway, involving many assembly factors. To better understand this process, we investigated native assembly intermediates of the mitoribosomal large subunit from the human parasite Trypanosoma brucei using cryo-electron microscopy. We identify 28 assembly factors, 6 of which are homologous to bacterial and eukaryotic ribosome assembly factors. They interact with the partially folded rRNA by specifically recognizing functionally important regions such as the peptidyltransferase center. The architectural and compositional comparison of the assembly intermediates indicates a stepwise modular assembly process, during which the rRNA folds toward its mature state. During the process, several conserved GTPases and a helicase form highly intertwined interaction networks that stabilize distinct assembly intermediates. The presented structures provide general insights into mitoribosomal maturation.
Identifiants
pubmed: 32679035
pii: S1097-2765(20)30432-9
doi: 10.1016/j.molcel.2020.06.030
pii:
doi:
Substances chimiques
RNA, Ribosomal
0
RNA, ribosomal, 12S
0
Ribosomal Proteins
0
GTP Phosphohydrolases
EC 3.6.1.-
DEAD-box RNA Helicases
EC 3.6.4.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
629-644.e4Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interests The authors declare no competing interests.