Publication details

Recognition of asymmetrically dimethylated arginine by TDRD3

Authors

ŠIKORSKÝ Tomáš HÓBOR Fruzsina KRIŽANOVÁ Eva PASULKA Josef KUBÍČEK Karel ŠTEFL Richard

Year of publication 2012
Type Article in Periodical
Magazine / Source Nucleic Acids Research
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://nar.oxfordjournals.org/content/40/22/11748.full-text-lowres.pdf
Doi http://dx.doi.org/10.1093/nar/gks929
Field Biophysics
Keywords tudor; assymetric dimethylarginine; histone; C-terminal domain of RNA polymerase II; recognition mark; nuclear magnetic resonance
Description Asymmetric dimethylarginine (aDMA) marks are placed on histones and the C-terminal domain (CTD) of RNA Polymerase II (RNAP II) and serve as a signal for recruitment of appropriate transcription and processing factors in coordination with transcription cycle. In contrast to other Tudor domain-containing proteins, Tudor domain-containing protein 3 (TDRD3) associates selectively with the aDMA marks but not with other methylarginine motifs. Here, we report the solution structure of the Tudor domain of TDRD3 bound to the asymmetrically dimethylated CTD. The structure and mutational analysis provide a molecular basis for how TDRD3 recognizes the aDMA mark. The unique aromatic cavity of the TDRD3 Tudor domain with a tyrosine in position 566 creates a selectivity filter for the aDMA residue. Our work contributes to the understanding of substrate selectivity rules of the Tudor aromatic cavity, which is an important structural motif for reading of methylation marks.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info