Recognition of asymmetrically dimethylated arginine by TDRD3

ŠIKORSKÝ, Tomáš, Fruzsina HÓBOR, Eva KRIŽANOVÁ, Josef PASULKA, Karel KUBÍČEK and Richard ŠTEFL. Recognition of asymmetrically dimethylated arginine by TDRD3. Nucleic Acids Research. Oxford: Oxford University Press, 2012, vol. 40, No 22, p. 11748-11755. ISSN 0305-1048. Available from: https://dx.doi.org/10.1093/nar/gks929.

Basic information

• Original name: Recognition of asymmetrically dimethylated arginine by TDRD3
• Name in Czech: Recognition of asymmetrically dimethylated arginine by TDRD3
• Authors: ŠIKORSKÝ, Tomáš (703 Slovakia, belonging to the institution), Fruzsina HÓBOR (348 Hungary, belonging to the institution), Eva KRIŽANOVÁ (703 Slovakia, belonging to the institution), Josef PASULKA (203 Czech Republic, belonging to the institution), Karel KUBÍČEK (203 Czech Republic, belonging to the institution) and Richard ŠTEFL (203 Czech Republic, guarantor, belonging to the institution).
• Edition: Nucleic Acids Research, Oxford, Oxford University Press, 2012, 0305-1048.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10610 Biophysics
• Country of publisher: United Kingdom of Great Britain and Northern Ireland
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 8.278
• RIV identification code: RIV/00216224:14740/12:00057639
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1093/nar/gks929
• UT WoS: 000313414800056
• Keywords in English: tudor; assymetric dimethylarginine; histone; C-terminal domain of RNA polymerase II; recognition mark; nuclear magnetic resonance
• Tags: ok, rivok
• Tags: International impact, Reviewed

Abstract

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.

Links

• ED1.1.00/02.0068, research and development project: Name: CEITEC - central european institute of technology
• GAP305/10/1490, research and development project: Name: Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu

Investor: Czech Science Foundation

• GBP305/12/G034, research and development project: Name: Centrum biologie RNA