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Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution

MPG-Autoren
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Habeck,  M
Department Empirical Inference, Max Planck Institute for Biological Cybernetics, Max Planck Society;
Max Planck Institute for Biological Cybernetics, Max Planck Society;

Externe Ressourcen

http://www.pnas.org/content/pnas/107/46/19748.full.pdf
(Verlagsversion)

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Zitation

Armache, J.-P., Jarasch, A., Anger, A., Villa, E., Becker, T., Bhushan, S., et al. (2010). Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution. Proceedings of the National Academy of Sciences of the United States of America, 107(46), 19748-19753. doi:10.1073/pnas.1009999107.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0013-BD5C-0
Zusammenfassung
Protein biosynthesis, the translation of the genetic code into polypeptides, occurs on ribonucleoprotein particles called ribosomes. Although X-ray structures of bacterial ribosomes are available, high-resolution structures of eukaryotic 80S ribosomes are lacking. Using cryoelectron microscopy and single-particle reconstruction, we have determined the structure of a translating plant (Triticum aestivum) 80S ribosome at 5.5-Å resolution. This map, together with a 6.1-Å map of a Saccharomyces cerevisiae 80S ribosome, has enabled us to model ∼98 of the rRNA. Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES–ES and r-protein–ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.