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Journal Article

Translation initiation factor eIF3b contains a nine-bladed beta-propeller and interacts with the 40S ribosomal subunit.

MPS-Authors
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Schell,  S.
Research Group of 3D Electron Cryo-Microscopy, MPI for Biophysical Chemistry, Max Planck Society;

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Chari,  A.
Research Group of 3D Electron Cryo-Microscopy, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

20433849.pdf
(Publisher version), 2MB

Supplementary Material (public)

20433849_Suppl_1.pdf
(Supplementary material), 12MB

20433849_Suppl_2.pdf
(Supplementary material), 14MB

Citation

Liu, Y., Neumann, P., Kuhle, B., Monecke, T., Schell, S., Chari, A., et al. (2014). Translation initiation factor eIF3b contains a nine-bladed beta-propeller and interacts with the 40S ribosomal subunit. Structure, 22(6), 923-930. doi:10.1016/j.str.2014.03.010.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-FEEE-0
Abstract
The multisubunit eukaryotic translation initiation factor 3, among which the subunit b (eIF3b) is a major scaffold protein, plays essential roles in protein synthesis. Here, we report the crystal structure of the WD40 domain of Chaetomium thermophilum eIF3b, revealing a nine-bladed beta-propeller fold. Sequence analysis indicates that this propeller architecture is common to all eIF3b orthologs. Revisiting the cryo-electron microscopy (cryo-EM) map of the 43S preinitiation complex suggests an interaction of the eIF3b with the 40S ribosomal subunit involving the ribosomal protein S9e and the 18S rRNA. This model is strongly supported by the direct binding of eIF3b to 40S ribosomes and to the isolated ribosomal protein rpS9e in vitro.