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Zeitschriftenartikel

Mechanism of eIF6-mediated inhibition of ribosomal subunit joining

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;

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Gartmann.pdf
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Zitation

Gartmann, M., Blau, M., Armache, J. P., Mielke, T., Topf, M., & Beckmann, R. (2010). Mechanism of eIF6-mediated inhibition of ribosomal subunit joining. The Journal of Biological Chemistry, 285(20), 14848-14851. doi:10.1074/jbc.C109.096057.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-7B14-C
Zusammenfassung
During the process of ribosomal assembly, the essential eukaryotic translation initiation factor 6 (eIF6) is known to act as a ribosomal anti-association factor. However, a molecular understanding of the anti-association activity of eIF6 is still missing. Here we present the cryo-electron microscopy reconstruction of a complex of the large ribosomal subunit with eukaryotic eIF6 from Saccharomyces cerevisiae. The structure reveals that the eIF6 binding site involves mainly rpL23 (L14p in Escherichia coli). Based on our structural data, we propose that the mechanism of the anti-association activity of eIF6 is based on steric hindrance of intersubunit bridge formation around the dynamic bridge B6.