Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
08 05 2023
08 05 2023
Historique:
accepted:
07
03
2023
revised:
02
03
2023
received:
09
02
2022
medline:
9
5
2023
pubmed:
24
3
2023
entrez:
23
3
2023
Statut:
ppublish
Résumé
The chemical modification of ribosomal RNA and proteins is critical for ribosome assembly, for protein synthesis and may drive ribosome specialisation in development and disease. However, the inability to accurately visualise these modifications has limited mechanistic understanding of the role of these modifications in ribosome function. Here we report the 2.15 Å resolution cryo-EM reconstruction of the human 40S ribosomal subunit. We directly visualise post-transcriptional modifications within the 18S rRNA and four post-translational modifications of ribosomal proteins. Additionally, we interpret the solvation shells in the core regions of the 40S ribosomal subunit and reveal how potassium and magnesium ions establish both universally conserved and eukaryote-specific coordination to promote the stabilisation and folding of key ribosomal elements. This work provides unprecedented structural details for the human 40S ribosomal subunit that will serve as an important reference for unravelling the functional role of ribosomal RNA modifications.
Identifiants
pubmed: 36951107
pii: 7084596
doi: 10.1093/nar/gkad194
pmc: PMC10164566
doi:
Substances chimiques
Ribosomal Proteins
0
RNA, Ribosomal
0
RNA, Ribosomal, 18S
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4043-4054Subventions
Organisme : Wellcome Trust
ID : 206171/Z/17/Z
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/T012412/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 202905/Z/16/Z
Pays : United Kingdom
Informations de copyright
© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.
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