Structural basis of signal-sequence recognition by the signal recognition particle (original) (raw)

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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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 toTobias Hainzl.

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The authors declare no competing financial interests.

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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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