Cryo-EM captures early ribosome assembly in action

Bo Qin, Simon M. Lauer, Annika Balke, Carlos H. Vieira-Vieira, Jörg Bürger, Thorsten Mielke, Matthias Selbach, Patrick Scheerer, Christian M. T. Spahn () and Rainer Nikolay ()
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Bo Qin: Institut für Medizinische Physik und Biophysik, Charité – Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität zu Berlin
Simon M. Lauer: Institut für Medizinische Physik und Biophysik, Charité – Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität zu Berlin
Annika Balke: Charité – Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction
Carlos H. Vieira-Vieira: Proteome Dynamics, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC)
Jörg Bürger: Institut für Medizinische Physik und Biophysik, Charité – Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität zu Berlin
Thorsten Mielke: Microscopy and Cryo-Electron Microscopy Service Group, Max Planck Institute for Molecular Genetics
Matthias Selbach: Proteome Dynamics, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC)
Patrick Scheerer: Charité – Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction
Christian M. T. Spahn: Institut für Medizinische Physik und Biophysik, Charité – Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität zu Berlin
Rainer Nikolay: Institut für Medizinische Physik und Biophysik, Charité – Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität zu Berlin

Nature Communications, 2023, vol. 14, issue 1, 1-10

Abstract: Abstract Ribosome biogenesis is a fundamental multi-step cellular process in all domains of life that involves the production, processing, folding, and modification of ribosomal RNAs (rRNAs) and ribosomal proteins. To obtain insights into the still unexplored early assembly phase of the bacterial 50S subunit, we exploited a minimal in vitro reconstitution system using purified ribosomal components and scalable reaction conditions. Time-limited assembly assays combined with cryo-EM analysis visualizes the structurally complex assembly pathway starting with a particle consisting of ordered density for only ~500 nucleotides of 23S rRNA domain I and three ribosomal proteins. In addition, our structural analysis reveals that early 50S assembly occurs in a domain-wise fashion, while late 50S assembly proceeds incrementally. Furthermore, we find that both ribosomal proteins and folded rRNA helices, occupying surface exposed regions on pre-50S particles, induce, or stabilize rRNA folds within adjacent regions, thereby creating cooperativity.

Date: 2023
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DOI: 10.1038/s41467-023-36607-9

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