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Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution.

Published version
Peer-reviewed

Repository DOI


Type

Article

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Authors

Dent, Kyle C 
Spikes, Tobias 

Abstract

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.

Description

Keywords

Humans, Ribosome Subunits, Small, Eukaryotic, Cryoelectron Microscopy, Ribosomal Proteins, Ribosomes, RNA, Ribosomal, RNA, Ribosomal, 18S

Journal Title

Nucleic Acids Res

Conference Name

Journal ISSN

0305-1048
1362-4962

Volume Title

Publisher

Oxford University Press (OUP)
Sponsorship
MRC (MR/T012412/1)
Wellcome Trust (202905/Z/16/Z)
Wellcome Trust (206171/Z/17/Z)
National Institute for Health and Care Research (IS-BRC-1215-20014)
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2023-06-29 10:43:56
Published version created
2023-03-09 00:30:41
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