Informace o publikaci

Recognition of asymmetrically dimethylated arginine by TDRD3

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

Rok publikování 2012
Druh Článek v odborném periodiku
Časopis / Zdroj Nucleic Acids Research
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://nar.oxfordjournals.org/content/40/22/11748.full-text-lowres.pdf
Doi http://dx.doi.org/10.1093/nar/gks929
Obor Biofyzika
Klíčová slova tudor; assymetric dimethylarginine; histone; C-terminal domain of RNA polymerase II; recognition mark; nuclear magnetic resonance
Popis 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.
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