Chromodomains read the arginine code of post-translational targeting.
Heidelberg, Germany. In Nat Struct Mol Biol, 2012
The authors 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.
Recognition of a signal peptide by the signal recognition particle.
Cambridge, United Kingdom. In Nature, 2010
A universally conserved component of SRP (refs 1, 2), SRP54 or its bacterial homologue, fifty-four homologue (Ffh), binds the signal peptides, which have a highly divergent sequence divisible into a positively charged n-region, an h-region commonly containing 8-20 hydrophobic residues and a polar c-region.
A structural step into the SRP cycle.
Heidelberg, Germany. In Mol Microbiol, 2004
The SRP core (SRP54 with its cognate RNA binding site) plays a central role in these interactions and communicates the different binding states by long-range interdomain communication.