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Structural basis of signal-sequence recognition by the signal recognition particle

Nature Structural & Molecular Biology volume 18, pages 389–391 (2011)Cite this article

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Abstract

The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-Å structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker helix and a 180° flip of the NG domain—structural changes that ensure a hierarchical succession of events during protein targeting.

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Figure 1: Structure of the M. jannaschii S domain of SRP in complex with a functional signal sequence.
Figure 2: Structural basis for signal-sequence recognition.
Figure 3: Signal-sequence induced structural changes in the SRP core.

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References

  1. Egea, P.F., Stroud, R.M. & Walter, P. Curr. Opin. Struct. Biol. 15, 213–220 (2005).

    Article  CAS  Google Scholar 

  2. Batey, R.T., Rambo, R.P., Lucast, L., Rha, B. & Doudna, J.A. Science 287, 1232–1239 (2000).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  4. Keenan, R.J., Freymann, D.M., Walter, P. & Stroud, R.M. Cell 94, 181–191 (1998).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  7. Peluso, P. et al. Science 288, 1640–1643 (2000).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  9. Lee, H.C. & Bernstein, H.D. Proc. Natl. Acad. Sci. USA 98, 3471–3476 (2001).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  11. Halic, M. et al. Nature 427, 808–814 (2004).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  13. Janda, C.Y. et al. Nature 465, 507–510 (2010).

    Article  CAS  Google Scholar 

  14. Hainzl, T., Huang, S. & Sauer-Eriksson, A.E. Nature 417, 767–771 (2002).

    Article  CAS  Google Scholar 

  15. Hainzl, T., Huang, S. & Sauer-Eriksson, A.E. Proc. Natl. Acad. Sci. USA 104, 14911–14916 (2007).

    Article  CAS  Google Scholar 

  16. Kuglstatter, A., Oubridge, C. & Nagai, K. Nat. Struct. Biol. 9, 740–744 (2002).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  18. Zhang, X., Kung, S. & Shan, S.O. J. Mol. Biol. 381, 581–593 (2008).

    Article  CAS  Google Scholar 

Download references

Acknowledgements

We thank the European Synchrotron Radiation Facility (Grenoble, France) for provision of synchrotron radiation facilities, and T. Bergfors and U. Sauer for critical reading of the manuscript. This work was supported by the Swedish Research Council (A.E.S.-E.) and Kempe Foundation (A.E.S.-E.).

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Authors and Affiliations

  1. Department of Chemistry, Umeå University, Umeå, Sweden

    Tobias Hainzl, Shenghua Huang, Gitte Meriläinen & A Elisabeth Sauer-Eriksson

  2. Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden

    Kristoffer Brännström

Authors
  1. Tobias Hainzl
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  2. Shenghua Huang
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  3. Gitte Meriläinen
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  4. Kristoffer Brännström
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  5. A Elisabeth Sauer-Eriksson
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Contributions

T.H., S.H. and A.E.S.-E. contributed to every aspect of this work. G.M. contributed to cloning and protein production and K.B. to Biacore experiments.

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Correspondence to Tobias Hainzl.

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The authors declare no competing financial interests.

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Supplementary Figures 1–7, Supplementary Table 1 and Supplementary Methods (PDF 793 kb)

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Hainzl, T., Huang, S., Meriläinen, G. et al. Structural basis of signal-sequence recognition by the signal recognition particle. Nat Struct Mol Biol 18, 389–391 (2011). https://doi.org/10.1038/nsmb.1994

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