Recognition of asymmetrically dimethylated arginine by TDRD3

J 2012

Recognition of asymmetrically dimethylated arginine by TDRD3

ŠIKORSKÝ, Tomáš, Fruzsina HÓBOR, Eva KRIŽANOVÁ, Josef PASULKA, Karel KUBÍČEK et. al.

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

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10610 Biophysics

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

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

Abstract

V originále

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

Citovat

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.

@article{1068202,
   author = {Šikorský, Tomáš and Hóbor, Fruzsina and Križanová, Eva and Pasulka, Josef and Kubíček, Karel and Štefl, Richard},
   article_location = {Oxford},
   article_number = {22},
   doi = {http://dx.doi.org/10.1093/nar/gks929},
   keywords = {tudor; assymetric dimethylarginine; histone; C-terminal domain of RNA polymerase II; recognition mark; nuclear magnetic resonance},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic Acids Research},
   title = {Recognition of asymmetrically dimethylated arginine by TDRD3},
   url = {http://nar.oxfordjournals.org/content/40/22/11748.full-text-lowres.pdf},
   volume = {40},
   year = {2012}
}

TY  - JOUR
ID  - 1068202
AU  - Šikorský, Tomáš - Hóbor, Fruzsina - Križanová, Eva - Pasulka, Josef - Kubíček, Karel - Štefl, Richard
PY  - 2012
TI  - Recognition of asymmetrically dimethylated arginine by TDRD3
JF  - Nucleic Acids Research
VL  - 40
IS  - 22
SP  - 11748-11755
EP  - 11748-11755
PB  - Oxford University Press
SN  - 03051048
KW  - tudor
KW  - assymetric dimethylarginine
KW  - histone
KW  - C-terminal domain of RNA polymerase II
KW  - recognition mark
KW  - nuclear magnetic resonance
UR  - http://nar.oxfordjournals.org/content/40/22/11748.full-text-lowres.pdf
L2  - http://nar.oxfordjournals.org/content/40/22/11748.full-text-lowres.pdf
N2  - 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.
ER  -

ŠIKORSKÝ, Tomáš, Fruzsina HÓBOR, Eva KRIŽANOVÁ, Josef PASULKA, Karel KUBÍČEK and Richard ŠTEFL. Recognition of asymmetrically dimethylated arginine by TDRD3. \textit{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.

Detailed Information on Publication Record