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Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor

Nature Structural & Molecular Biology volume 18, pages 88–90 (2011)Cite this article

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Abstract

We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the tetraloop of the SRP RNA, whereas the NG domains of the SRP protein and FtsY interact weakly in this conformation. Our results suggest that optimal positioning of the SRP RNA tetraloop and the Ffh NG domain leads to FtsY recruitment.

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Figure 1: Generation and characterization of RNC–SRP–FtsY.
Figure 2: Atomic model of the early conformation of scSRP.
Figure 3: Cartoon model of co-translational targeting.

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References

  1. Walter, P. & Johnson, A.E. Annu. Rev. Cell Biol. 10, 87–119 (1994).

    Article  CAS  Google Scholar 

  2. Nagai, K. et al. EMBO J. 22, 3479–3485 (2003).

    Article  CAS  Google Scholar 

  3. Doudna, J.A. & Batey, R.T. Annu. Rev. Biochem. 73, 539–557 (2004).

    Article  CAS  Google Scholar 

  4. Ulbrandt, N.D., Newitt, J.A. & Bernstein, H.D. Cell 88, 187–196 (1997).

    Article  CAS  Google Scholar 

  5. Freymann, D.M., Keenan, R.J., Stroud, R.M. & Walter, P. Nature 385, 361–364 (1997).

    Article  CAS  Google Scholar 

  6. Montoya, G., Svensson, C., Luirink, J. & Sinning, I. Nature 385, 365–368 (1997).

    Article  CAS  Google Scholar 

  7. Connolly, T., Rapiejko, P. & Gilmore, R. Science 252, 1171–1173 (1991).

    Article  CAS  Google Scholar 

  8. Focia, P.J., Shepotinovskaya, I.V., Seidler, J.A. & Freymann, D.M. Science 303, 373–377 (2004).

    Article  CAS  Google Scholar 

  9. Egea, P.F. et al. Nature 427, 215–221 (2004).

    Article  CAS  Google Scholar 

  10. Batey, R.T. et al. Science 287, 1232–1239 (2000).

    Article  CAS  Google Scholar 

  11. Weiche, B. et al. J. Mol. Biol. 377, 761–773 (2008).

    Article  CAS  Google Scholar 

  12. Zhang, X., Schaffitzel, C., Ban, N. & Shan, S.O. Proc. Natl. Acad. Sci. USA 106, 1754–1759 (2009).

    Article  CAS  Google Scholar 

  13. Schaffitzel, C. et al. Nature 444, 503–506 (2006).

    Article  CAS  Google Scholar 

  14. Halic, M. et al. Nature 444, 507–511 (2006).

    Article  CAS  Google Scholar 

  15. Schuwirth, B.S. et al. Science 310, 827–834 (2005).

    Article  CAS  Google Scholar 

  16. Shen, K. & Shan, S.O. Proc. Natl. Acad. Sci. USA 107, 7698–7703 (2010).

    Article  CAS  Google Scholar 

  17. Jagath, J.R. et al. RNA 7, 293–301 (2001).

    Article  CAS  Google Scholar 

  18. Siu, F.Y., Spanggord, R.J. & Doudna, J.A. RNA 13, 240–250 (2007).

    Article  CAS  Google Scholar 

  19. Halic, M. et al. Science 312, 745–747 (2006).

    Article  CAS  Google Scholar 

  20. Bradshaw, N., Neher, S.B., Booth, D.S. & Walter, P. Science 323, 127–130 (2009).

    Article  CAS  Google Scholar 

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Acknowledgements

We would like to thank G. Schoehn for collecting EM data, I. Berger for designing scSRP, C. Frick for technical assistance and X. Zhang for helpful suggestions. W. Wintermeyer (Max Planck Institute for Biophysical Chemistry) kindly provided pET24a-Ffh. J. Luirink (Vrije Universiteit Amsterdam) is acknowledged for providing pET9-FtsY. This work was supported by the Swiss National Science Foundation (SNSF) and the National Center of Excellence in Research Structural Biology program of the SNSF. The authors acknowledge support by the Electron Microscopy of ETH Zurich (EMEZ) and from the infrastructure of the Partnership for Structural Biology in Grenoble.

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Author notes

  1. Leandro F Estrozi and Daniel Boehringer: These authors contributed equally to this work.

Authors and Affiliations

  1. European Molecular Biology Laboratory, Grenoble Outstation, Grenoble, France

    Leandro F Estrozi & Christiane Schaffitzel

  2. Unit of Virus Host-Cell Interactions, Unité Mixte Internationale 3265, Grenoble, France

    Leandro F Estrozi & Christiane Schaffitzel

  3. ETH Zurich (Swiss Federal Institute of Technology), Institute of Molecular Biology and Biophysics, Zurich, Switzerland

    Daniel Boehringer & Nenad Ban

  4. Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, USA

    Shu-ou Shan

Authors
  1. Leandro F Estrozi
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  2. Daniel Boehringer
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  3. Shu-ou Shan
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  4. Nenad Ban
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  5. Christiane Schaffitzel
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Contributions

C.S. conceived the scSRP construct and performed sample preparations; S.-o.S. performed activity assays; D.B. did the electron microscopy; D.B., L.F.E. and C.S. performed the image analysis and model building; C.S., N.B., D.B. and S.-o.S. prepared the manuscript.

Corresponding authors

Correspondence to Nenad Ban or Christiane Schaffitzel.

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The authors declare no competing financial interests.

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Supplementary Figures 1–5, Supplementary Methods and Supplementary Discussion (PDF 738 kb)

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Estrozi, L., Boehringer, D., Shan, So. et al. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nat Struct Mol Biol 18, 88–90 (2011). https://doi.org/10.1038/nsmb.1952

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