About: Recognition of asymmetrically dimethylated arginine by TDRD3

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About: Recognition of asymmetrically dimethylated arginine by TDRD3 Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://nar.oxfordjournals.org/content/40/22/11748.full-text-lowres.pdf
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. 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. (en)
Title	Recognition of asymmetrically dimethylated arginine by TDRD3 Recognition of asymmetrically dimethylated arginine by TDRD3 (en)
skos:prefLabel	Recognition of asymmetrically dimethylated arginine by TDRD3 Recognition of asymmetrically dimethylated arginine by TDRD3 (en)
skos:notation	RIV/00216224:14740/12:00057639!RIV13-GA0-14740___
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(ED1.1.00/02.0068), P(GAP305/10/1490), P(GBP305/12/G034)
http://linked.open...iv/cisloPeriodika	22
http://linked.open...vai/riv/dodaniDat	2013
http://linked.open...aciTvurceVysledku	Kubíček, Karel Štefl, Richard Pasulka, Josef Šikorský, Tomáš Križanová, Eva Hóbor, Fruzsina
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	164394
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/12:00057639
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	tudor; assymetric dimethylarginine; histone; C-terminal domain of RNA polymerase II; recognition mark; nuclear magnetic resonance (en)
http://linked.open.../riv/klicoveSlovo	nuclear magnetic resonance C-terminal domain of RNA polymerase II assymetric dimethylarginine histone recognition mark tudor
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[D54C5482A4CF]
http://linked.open...i/riv/nazevZdroje	Nucleic Acids Research
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	6 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...vavai/riv/projekt	Centre for RNA Biology Central european institute of technology Structural basis for poly(A) independent transcription termination pathway
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	40
http://linked.open...iv/tvurceVysledku	Kubíček, Karel Hóbor, Fruzsina Pasulka, Josef Štefl, Richard Šikorský, Tomáš Križanová, Eva
http://linked.open...ain/vavai/riv/wos	000313414800056
issn	0305-1048
number of pages	8 (xsd:int)
http://bibframe.org/vocab/doi	10.1093/nar/gks929
http://localhost/t...ganizacniJednotka	14740

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