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Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution
Open accessPreprint — published as 10.1093/nar/gkad194
Abstract
The chemical modification of ribosomal RNA and proteins is critical for ribosome assembly, for protein synthesis and may drive ribosome specialization in development and disease. However, the inability to accurately visualize 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 visualize post-transcriptional modifications within the 18S rRNA and post-translational modifications at the N-termini of two 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 stabilization 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 unraveling the functional role of ribosomal RNA modifications.
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Metadata
- Authors
- Pellegrino, S., Dent, K. C., Spikes, T., & Warren, A. J.
- Affiliations
- Wellcome/MRC Cambridge Stem Cell Institute (GB)
- Corresponding author
- Pellegrino, Simone
- Warren, Alan J.
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2022-01-16
- OpenAlex
- W4206411447
- Cited by
- 3
- References
- 2
- Citations by year
- 2022: 3
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Funders
- Wellcome Trust (206171/Z/17/Z, Z/17/Z, 202905, 100140, 202905/Z/16/Z, 206171)
- NIHR Biomedical Research Centre, Royal Marsden NHS Foundation Trust/Institute of Cancer Research
- National Institute for Health and Care Research
- Kay Kendall Leukaemia Fund
- University of Cambridge
- Blood Cancer UK (12048)
- Directorate for Biological Sciences
- Medical Research Council (MC_U105161083, MR/T012412/1)
- Cambridge Institute for Medical Research, University of Cambridge (100140)
- Department of Biochemistry, University of Cambridge
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- 40S ribosomal subunit, human ribosome, post-transcriptional modification, post-translational modification, solvation shell, potassium ion coordination, magnesium coordination, ribosome assembly, ribosome structure
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