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Chromodomains read the arginine code of post-translational targeting

Nature Structural & Molecular Biology volume 19, pages 260263 (2012) | Download Citation

Abstract

Chromodomains typically recruit protein complexes to chromatin and read the epigenetic histone code by recognizing lysine methylation in histone tails. We report the crystal structure of the chloroplast signal recognition particle (cpSRP) core from Arabidopsis thaliana, with the cpSRP54 tail comprising an arginine-rich motif bound to the second chromodomain of cpSRP43. A twinned aromatic cage reads out two neighboring nonmethylated arginines and adapts chromodomains to a non-nuclear function in post-translational targeting.

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Acknowledgements

This work was supported by grants from the Deutsche Forschungsgemeinschaft (DFG) SFB638 and the Graduiertenkolleg GRK1188 (to I.S.). We thank J. Kopp and C. Siegmann from the crystallization platform of the Biochemiezentrum der Universität Heidelberg (BZH)/Cluster of Excellence:CellNetworks for support in protein crystallization, R. Lindner for support in evolutionary analysis, and S. Falk, G. Bange and D. Schünemann for stimulating discussions. We acknowledge the European Synchrotron Radiation Facility for providing synchrotron radiation and for assistance in using beamlines ID14eh2 and ID14eh3. M.S. and H.M. acknowledge support from the Cluster of Excellence, Center for integrated Protein Science, Munich (CiPSM). I.S. is an investigator of the Cluster of Excellence:CellNetworks.

Author information

Affiliations

  1. Heidelberg University Biochemistry Center, Heidelberg, Germany.

    • Iris Holdermann
    • , Klemens Wild
    •  & Irmgard Sinning
  2. Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany.

    • N Helge Meyer
    •  & Michael Sattler
  3. Munich Center for Integrated Protein Science and Chair of Biomolecular NMR, Department Chemie, Technische Universität München, Garching, Germany.

    • N Helge Meyer
    •  & Michael Sattler
  4. European Molecular Biology Laboratory, Grenoble Outstation, Grenoble, France.

    • Adam Round

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Contributions

I.H., K.W. and I.S. designed experiments and analyzed the data. I.H. conducted experiments. N.H.M. and M.S. provided NMR spectroscopy data and analysis. A.R. processed and analyzed SAXS data. I.H., K.W. and I.S. wrote the manuscript. All authors commented on the manuscript.

Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Irmgard Sinning.

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    Supplementary Figures 1–7, Supplementary Tables 1 and 2 and Supplementary Methods

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DOI

https://doi.org/10.1038/nsmb.2196

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