Affiliation:
1. Department of Haematology, University of Cambridge , Hills Road , Cambridge CB2 0XY, UK
2. Cambridge Institute for Medical Research , Keith Peters Building, Hills Road , Cambridge CB2 0XY, UK
3. Wellcome Trust–Medical Research Council Stem Cell Institute, University of Cambridge , Cambridge , UK
Abstract
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.
Funder
Kay Kendall Leukaemia Fund
UK Medical Research Council
European Cooperation in Science and Technology
European Network for Innovative Diagnosis and treatment of Chronic Neutropenias, INNOCHRON
Translational control in Cancer European Network, TRANSLACORE
MRC
Cambridge National Institute for Health Research Biomedical Research Centre
Wellcome Trust
Departments of Biochemistry and Chemistry
Schools of Biological Sciences and Clinical Medicine
University of Cambridge
Publisher
Oxford University Press (OUP)
Cited by
3 articles.
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