Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM

Timo Flügel, Magdalena Schacherl, Anett Unbehaun, Birgit Schroeer, Marylena Dabrowski, Jörg Bürger, Thorsten Mielke, Thiemo Sprink, Christoph A. Diebolder, Yollete V. Guillén Schlippe () and Christian M. T. Spahn ()
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Timo Flügel: Institute of Medical Physics and Biophysics
Magdalena Schacherl: Institute of Medical Physics and Biophysics
Anett Unbehaun: Institute of Medical Physics and Biophysics
Birgit Schroeer: Institute of Medical Physics and Biophysics
Marylena Dabrowski: Institute of Medical Physics and Biophysics
Jörg Bürger: Institute of Medical Physics and Biophysics
Thorsten Mielke: Microscopy and Cryo-Electron Microscopy Service Group
Thiemo Sprink: Charité — Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin
Christoph A. Diebolder: Charité — Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin
Yollete V. Guillén Schlippe: Institute of Medical Physics and Biophysics
Christian M. T. Spahn: Institute of Medical Physics and Biophysics

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract Structural studies of translating ribosomes traditionally rely on in vitro assembly and stalling of ribosomes in defined states. To comprehensively visualize bacterial translation, we reactivated ex vivo-derived E. coli polysomes in the PURE in vitro translation system and analyzed the actively elongating polysomes by cryo-EM. We find that 31% of 70S ribosomes assemble into disome complexes that represent eight distinct functional states including decoding and termination intermediates, and a pre-nucleophilic attack state. The functional diversity of disome complexes together with RNase digest experiments suggests that paused disome complexes transiently form during ongoing elongation. Structural analysis revealed five disome interfaces between leading and queueing ribosomes that undergo rearrangements as the leading ribosome traverses through the elongation cycle. Our findings reveal at the molecular level how bL9’s CTD obstructs the factor binding site of queueing ribosomes to thwart harmful collisions and illustrate how translation dynamics reshape inter-ribosomal contacts.

Date: 2024
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DOI: 10.1038/s41467-024-46092-3

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