About: Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1

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About: Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1 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://www.ncbi.nlm.nih.gov/pubmed/22892239
Description	Recruitment of appropriate RNA processing factors to the site of transcription is controlled by post-translational modifications of the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Here, we report the solution structure of the Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream pSer5–Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface diminish binding affinity and impair processing or degradation of noncoding RNAs. These findings underpin the interplay between covalent and noncovalent changes in the CTD structure that constitute the CTD code. Recruitment of appropriate RNA processing factors to the site of transcription is controlled by post-translational modifications of the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Here, we report the solution structure of the Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream pSer5–Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface diminish binding affinity and impair processing or degradation of noncoding RNAs. These findings underpin the interplay between covalent and noncovalent changes in the CTD structure that constitute the CTD code. (en)
Title	Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1 Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1 (en)
skos:prefLabel	Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1 Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1 (en)
skos:notation	RIV/00216224:14740/12:00057508!RIV13-GA0-14740___
http://linked.open...avai/predkladatel	Středoevropský technologický institut
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(ED1.1.00/02.0068), P(GAP205/12/0550), P(GAP305/10/1490), P(GAP305/11/1095), P(GBP305/12/G034)
http://linked.open...iv/cisloPeriodika	17
http://linked.open...vai/riv/dodaniDat	2013
http://linked.open...aciTvurceVysledku	Kubíček, Karel Vaňáčová, Štěpánka Štefl, Richard Pasulka, Josef Hroššová, Dominika Hofr, Ctirad Černá, Hana Holub, Peter
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	167542
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/12:00057508
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	RNA polymerase II; CTD code; phosphorylation; proline isomerization; RNA processing and degradation; NMR spectroscopy; structure (en)
http://linked.open.../riv/klicoveSlovo	NMR spectroscopy structure CTD code RNA polymerase II RNA processing and degradation proline isomerization phosphorylation
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[379E8D1954DB]
http://linked.open...i/riv/nazevZdroje	Genes & Development
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	8 (xsd:int)
http://linked.open...cetTvurcuVysledku	9 (xsd:int)
http://linked.open...vavai/riv/projekt	Functional and biochemical characterization of Dis3L2, the third mammalian homolog of the key yeast exosome nuclease Dis3p Centre for RNA Biology Central european institute of technology Dynamics of shelterin complex assembly Structural basis for poly(A) independent transcription termination pathway
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	26
http://linked.open...iv/tvurceVysledku	Černá, Hana Kubíček, Karel Hofr, Ctirad Hroššová, Dominika Pasulka, Josef Vaňáčová, Štěpánka Štefl, Richard Holub, Peter Loehr, Frank
http://linked.open...ain/vavai/riv/wos	000308391800002
issn	0890-9369
number of pages	6 (xsd:int)
http://bibframe.org/vocab/doi	10.1101/gad.192781.112
http://localhost/t...ganizacniJednotka	14740
is http://linked.open...avai/riv/vysledek of	Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1

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