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.
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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.
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Supplementary Figures 1–7, Supplementary Tables 1 and 2 and Supplementary Methods (PDF 10415 kb)
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Holdermann, I., Meyer, N., Round, A. et al. Chromodomains read the arginine code of post-translational targeting. Nat Struct Mol Biol 19, 260–263 (2012). https://doi.org/10.1038/nsmb.2196
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DOI: https://doi.org/10.1038/nsmb.2196
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