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.

Základní údaje

Originální název

Recognition of asymmetrically dimethylated arginine by TDRD3

Název česky

Recognition of asymmetrically dimethylated arginine by TDRD3

Autoři

ŠIKORSKÝ, Tomáš (703 Slovensko, domácí), Fruzsina HÓBOR (348 Maďarsko, domácí), Eva KRIŽANOVÁ (703 Slovensko, domácí), Josef PASULKA (203 Česká republika, domácí), Karel KUBÍČEK (203 Česká republika, domácí) a Richard ŠTEFL (203 Česká republika, garant, domácí)

Vydání

Nucleic Acids Research, Oxford, Oxford University Press, 2012, 0305-1048

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10610 Biophysics

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 8.278

Kód RIV

RIV/00216224:14740/12:00057639

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1093/nar/gks929

UT WoS

000313414800056

Klíčová slova anglicky

tudor; assymetric dimethylarginine; histone; C-terminal domain of RNA polymerase II; recognition mark; nuclear magnetic resonance

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 12. 4. 2013 08:01, Olga Křížová

Anotace

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GAP305/10/1490, projekt VaV

Název: Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu

Investor: Grantová agentura ČR, Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu

GBP305/12/G034, projekt VaV

Název: Centrum biologie RNA

Citovat

ŠIKORSKÝ, Tomáš, Fruzsina HÓBOR, Eva KRIŽANOVÁ, Josef PASULKA, Karel KUBÍČEK a Richard ŠTEFL. Recognition of asymmetrically dimethylated arginine by TDRD3. Nucleic Acids Research. Oxford: Oxford University Press, 2012, roč. 40, č. 22, s. 11748-11755. ISSN 0305-1048. Dostupné z: 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 a Richard ŠTEFL. Recognition of asymmetrically dimethylated arginine by TDRD3. \textit{Nucleic Acids Research}. Oxford: Oxford University Press, 2012, roč.~40, č.~22, s.~11748-11755. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gks929.

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