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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50431

Mielke,  T.
Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50642

Wilson,  D. N.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Armache.pdf
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Zitation

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


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-79EC-5
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-A resolution. This map, together with a 6.1-A map of a Saccharomyces cerevisiae 80S ribosome, has enabled us to model approximately 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.