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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
Language
english
Publication Year
2012
HGF-reported in Year
2012
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
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-503000-001
PubMed ID
22231402
WOS ID
WOS:000300029400021
Scopus ID
84856738261
Erfassungsdatum
2012-03-06