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Structures of the eukaryotic ribosome and its translational states in situ

MPG-Autoren
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Hoffmann,  Patrick C.       
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Kreysing,  Jan Philipp       
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;
IMPRS-CBP, Max Planck Institute of Biophysics, Max Planck Society;

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Khusainov,  Iskander       
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Tuijtel,  Maarten       
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Welsch,  Sonja       
Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society;

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Beck,  Martin       
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Hoffmann, P. C., Kreysing, J. P., Khusainov, I., Tuijtel, M., Welsch, S., & Beck, M. (2022). Structures of the eukaryotic ribosome and its translational states in situ. Nature Communications, 13: 7435. doi:10.1038/s41467-022-34997-w.


Zitierlink: https://hdl.handle.net/21.11116/0000-000B-B2D0-0
Zusammenfassung
Ribosomes translate genetic information into primary structure. During translation, various cofactors transiently bind to the ribosome that undergoes prominent conformational and structural changes. Different translational states of ribosomes have been well characterized in vitro. However, to which extent the known translational states are representative of the native situation inside cells has thus far only been addressed in prokaryotes. Here, we apply cryo-electron tomography to cryo-FIB milled Dictyostelium discoideum cells combined with subtomogram averaging and classification. We obtain an in situ structure that is locally resolved up to 3 Angstrom, the distribution of eukaryotic ribosome translational states, and unique arrangement of rRNA expansion segments. Our work demonstrates the use of in situ structural biology techniques for identifying distinct ribosome states within the cellular environment.