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Structure of a Yeast 40S–eIF1–eIF1A–eIF3–eIF3j initiation complex

Nature Structural & Molecular Biology volume 22, pages 269271 (2015) | Download Citation

Abstract

Eukaryotic translation initiation requires cooperative assembly of a large protein complex at the 40S ribosomal subunit. We have resolved a budding yeast initiation complex by cryo-EM, allowing placement of prior structures of eIF1, eIF1A, eIF3a, eIF3b and eIF3c. Our structure highlights differences in initiation-complex binding to the ribosome compared to that of mammalian eIF3, demonstrates a direct contact between eIF3j and eIF1A and reveals the network of interactions between eIF3 subunits.

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Acknowledgements

We would like to thank the ETH Zürich Scientific Center for Optical and Electron Microscopy for access to EM equipment and are indebted to P. Tittmann for technical support. C.H.S.A. was supported by an ETH Zürich postdoctoral fellowship and an European Molecular Biology Organization (EMBO) long-term fellowship and J.P.E. by an EMBO long-term fellowship. This work was supported by the Swiss National Science Foundation (SNSF), the National Center of Excellence in Research (of Switzerland), the Structural Biology, and RNA and Disease programs of the SNSF and European Research Council grant 250071 (to N.B.) under the European Community's Seventh Framework Programme.

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Affiliations

  1. Institute for Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zürich, Zürich, Switzerland.

    • Christopher H S Aylett
    • , Daniel Boehringer
    • , Jan P Erzberger
    • , Tanja Schaefer
    •  & Nenad Ban

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Contributions

N.B. and C.H.S.A. designed the study. C.H.S.A., J.P.E. and T.S. prepared samples and performed biochemical experiments. C.H.S.A. and D.B. collected electron micrographs and calculated reconstructions. C.H.S.A., D.B., J.P.E. and N.B. interpreted the structures and wrote the manuscript.

Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Nenad Ban.

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DOI

https://doi.org/10.1038/nsmb.2963

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