Chromodomains read the arginine code of post-translational targeting
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 compris...
Gespeichert in:
| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
08 January 2012
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| In: |
Nature structural & molecular biology
Year: 2012, Jahrgang: 19, Heft: 2, Pages: 260-263 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb.2196 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1038/nsmb.2196 Verlag, Volltext: https://www.nature.com/articles/nsmb.2196 
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| Verfasserangaben: | Iris Holdermann, N Helge Meyer, Adam Round, Klemens Wild, Michael Sattler & Irmgard Sinning |
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| 520 | |a 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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