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Lookup NU author(s): Karla Helena Bueno, Lewis Chan, Dr Arnaud Basle, Dr Sergey MelnikovORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© The Author(s) 2025. Ribosome heterogeneity is a paradigm in biology, pertaining to the existence of structurally distinct populations of ribosomes within a single organism or cell. This concept suggests that structurally distinct pools of ribosomes have different functional properties and may be used to translate specific mRNAs. However, it is unknown to what extent structural heterogeneity reflects genuine functional specialization rather than stochastic variations in ribosome assembly. Here, we address this question by combining cryo-electron microscopy and tomography to observe individual structurally heterogeneous ribosomes in bacterial cells. We show that 70% of ribosomes in Psychrobacter urativorans contain a second copy of the ribosomal protein bS20 at a previously unknown binding site on the large ribosomal subunit. We then determine that this second bS20 copy appears to be functionally neutral. This demonstrates that ribosome heterogeneity does not necessarily lead to functional specialization, even when it involves significant variations such as the presence or absence of a ribosomal protein. Instead, we show that heterogeneous ribosomes can cooperate in general protein synthesis rather than specialize in translating discrete populations of mRNA.
Author(s): Helena-Bueno K, Kopetschke S, Filbeck S, Chan LI, Birsan S, Basle A, Hudson M, Pfeffer S, Hill CH, Melnikov SV
Publication type: Article
Publication status: Published
Journal: Nature Communications
Year: 2025
Volume: 16
Online publication date: 20/03/2025
Acceptance date: 05/03/2025
Date deposited: 09/04/2025
ISSN (electronic): 2041-1723
Publisher: Springer Nature
URL: https://doi.org/10.1038/s41467-025-57955-8
DOI: 10.1038/s41467-025-57955-8
Data Access Statement: The atomic coordinate file for the structure of P. urativorans ribosomes with two copies of bS20 generated in this study has been deposited in the Protein Data Bank (PDB) with the accession code 9HC4. The associated cryo-EM maps generated in this study were deposited to the Electron Microscopy Data Bank (EMDB) with the accession codes EMD-52036 (cryo-EM reconstruction of 2xbS20 ribosomes), EMD-52351 (subtomogram average of all ribosomes), EMD-52352 (subtomogram average of 1xbS20 ribosomes) and EMD-52354 (subtomogram average of 2xbS20 ribosomes). A representative tomogram has been deposited to the EMDB with the accession code EMD-52842. Source data are provided with this paper.
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