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Crystal structure of the cpSRP54 tail bound to cpSRP43Crystal structure of the cpSRP54 tail bound to cpSRP43
Structural highlights
Publication Abstract from PubMedChromodomains 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. Chromodomains read the arginine code of post-translational targeting.,Holdermann I, Meyer NH, Round A, Wild K, Sattler M, Sinning I Nat Struct Mol Biol. 2012 Jan 8;19(2):260-3. doi: 10.1038/nsmb.2196. PMID:22231402[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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