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Open Access Green as soon as Postprint is submitted to ZB.
Chromodomains read the arginine code of post-translational targeting.
Nat. Struct. Mol. Biol. 19, 260-263 (2012)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Signal recognition particle; Histone H3; Protein; CPSRP43; Component; Binding; Domain
ISSN (print) / ISBN
1545-9993
e-ISSN
1545-9985
Quellenangaben
Volume: 19,
Issue: 2,
Pages: 260-263
Publisher
Nature Publishing Group
Publishing Place
New York, NY
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)