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 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.
Heidelberg University Biochemistry Center, Heidelberg, Germany.
Iris
I
Holdermann
N Helge
NH
Meyer
Adam
A
Round
Klemens
K
Wild
Michael
M
Sattler
Irmgard
I
Sinning
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism; D001120:Arginine / Q000378:metabolism*; D002843:Chromatin / Q000378:metabolism; D018360:Crystallography, X-Ray; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D018271:Signal Recognition Particle / Q000737:chemistry* / Q000378:metabolism
D029681:Arabidopsis Proteins; D002843:Chromatin; D006657:Histones; C091479:SRP54A protein, Arabidopsis; D018271:Signal Recognition Particle; C568473:cpSRP43 protein, Arabidopsis; D001120:Arginine; D019204:GTP-Binding Proteins