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

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Item Type:Article
Title:Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM
Creators Name:Flügel, T. and Schacherl, M. and Unbehaun, A. and Schroeer, B. and Dabrowski, M. and Bürger, J. and Mielke, T. and Sprink, T. and Diebolder, C.A. and Guillén Schlippe, Y.V. and Spahn, C.M.T.
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.
Keywords:Cryoelectron Microscopy, Escherichia coli, Polyribosomes, Protein Biosynthesis, Ribosomes / Metabolism
Source:Nature Communications
Publisher:Nature Publishing Group
Page Range:1756
Date:26 February 2024
Official Publication:https://doi.org/10.1038/s41467-024-46092-3
PubMed:View item in PubMed

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