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

View ORCID ProfileSimone Pellegrino, Kyle C. Dent, Tobias Spikes, View ORCID ProfileAlan J. Warren
doi: https://doi.org/10.1101/2022.01.16.475527
Simone Pellegrino
1Department of Haematology, University of Cambridge, Hills Road, Cambridge, CB2 0XY, UK
2Cambridge Institute for Medical Research, Keith Peters Building, Hills Road, Cambridge, CB2 0XY, UK
3Wellcome Trust–Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, UK
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  • ORCID record for Simone Pellegrino
  • For correspondence: sp946@cam.ac.uk ajw1000@cam.ac.uk
Kyle C. Dent
1Department of Haematology, University of Cambridge, Hills Road, Cambridge, CB2 0XY, UK
2Cambridge Institute for Medical Research, Keith Peters Building, Hills Road, Cambridge, CB2 0XY, UK
3Wellcome Trust–Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, UK
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Tobias Spikes
1Department of Haematology, University of Cambridge, Hills Road, Cambridge, CB2 0XY, UK
2Cambridge Institute for Medical Research, Keith Peters Building, Hills Road, Cambridge, CB2 0XY, UK
3Wellcome Trust–Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, UK
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Alan J. Warren
1Department of Haematology, University of Cambridge, Hills Road, Cambridge, CB2 0XY, UK
2Cambridge Institute for Medical Research, Keith Peters Building, Hills Road, Cambridge, CB2 0XY, UK
3Wellcome Trust–Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, UK
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  • ORCID record for Alan J. Warren
  • For correspondence: sp946@cam.ac.uk ajw1000@cam.ac.uk
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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.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted January 16, 2022.
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Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution
Simone Pellegrino, Kyle C. Dent, Tobias Spikes, Alan J. Warren
bioRxiv 2022.01.16.475527; doi: https://doi.org/10.1101/2022.01.16.475527
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Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution
Simone Pellegrino, Kyle C. Dent, Tobias Spikes, Alan J. Warren
bioRxiv 2022.01.16.475527; doi: https://doi.org/10.1101/2022.01.16.475527

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