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

Armache, J.-P., Jarasch A, Anger AM, Villa E, Becker T, Bhushan S, Jossinet F, Habeck, M., Dindar G, Franckenberg S, Marquez V, Mielke T, Thomm M, Berninghausen O, Beatrix B, Söding J, Westhof E, Wilson, D., & Beckmann, R. (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.

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Armache, J-P, Autor
Jarasch A, Anger AM, Villa E, Becker T, Bhushan S, Jossinet F, Habeck, M1, Autor           
Dindar G, Franckenberg S, Marquez V, Mielke T, Thomm M, Berninghausen O, Beatrix B, Söding J, Westhof E, Wilson, DN, Autor
Beckmann, R, Autor
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1Department Empirical Inference, Max Planck Institute for Biological Cybernetics, Max Planck Society, ou_1497795              

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 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.

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 Datum: 2010-11
 Publikationsstatus: Erschienen
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 Identifikatoren: URI: http://www.pnas.org/content/107/46/19748.full.pdf+html
DOI: 10.1073/pnas.1009999107
BibTex Citekey: ArmacheJAVBBJHDFMMTBBSWWB2011
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Titel: Proceedings of the National Academy of Sciences of the United States of America
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 107 (46) Artikelnummer: - Start- / Endseite: 19748 - 19753 Identifikator: -