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The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A

Abstract

Eukaryotic translation initiation factors (eIFs) 1A and 1 are central players in the complex process of start-codon recognition. To improve mechanistic understanding of this process, we determined the crystal structure of the 40S ribosomal subunit in complex with eIF1A and eIF1 from Tetrahymena thermophila at a resolution of 3.7 Å. It reveals the positions of the two factors on the 40S and the conformational changes that accompany their binding.

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Figure 1: eIF1A and eIF1 bound to the 40S subunit.
Figure 2: Rearrangements and interactions in the 40S–eIF1–eIF1A complex.

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Acknowledgements

All data were collected at the Swiss Light Source (SLS, Paul Scherrer Institut, Villigen). We thank T. Tomizaki, M. Müller, V. Olieric, M. Wang, C. Pradervand, M. Marsh and A. Pauluhn for their outstanding support at the SLS; A. Haag for advice on cell growth, ribosome purification and eIF cloning and purification; V. Hozjan and F. Benning for experimental support; and D. Böhringer, B. Greber and A. Casañas for critical reading of the manuscript. This work was supported by the Swiss National Science Foundation (SNSF) (grant 31003A 144214 to N.B.), the National Center of Excellence in Research Structural Biology program of the SNSF (N.B.) and the European Community's Seventh Framework Programme (Project PF7 250071 to N.B.).

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Contributions

J.R. cloned the initiation factors. M.W. and J.R. purified the initiation factors. M.W. crystallized the eIF1–eIF1A–40S complex. M.W. and M.L. solved the crystal structure. M.W., M.L., F.V.-H. and N.B. analyzed the data, interpreted the structure and wrote the manuscript.

Corresponding author

Correspondence to Nenad Ban.

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The authors declare no competing financial interests.

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Supplementary Figures 1–5 and Supplementary Tables 1–3 (PDF 10686 kb)

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Weisser, M., Voigts-Hoffmann, F., Rabl, J. et al. The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A. Nat Struct Mol Biol 20, 1015–1017 (2013). https://doi.org/10.1038/nsmb.2622

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  • DOI: https://doi.org/10.1038/nsmb.2622

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