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Statements

Subject Item
n2:RIV%2F00216224%3A14740%2F14%3A00073612%21RIV15-MSM-14740___
rdf:type
skos:Concept n19:Vysledek
rdfs:seeAlso
http://nar.oxfordjournals.org/content/early/2014/05/23/nar.gku446.long
dcterms:description
In Saccharomyces cerevisiae, the Nrd1-dependent termination and processing pathways play an important role in surveillance and processing of non-coding ribonucleic acids (RNAs). The termination and subsequent processing is dependent on the Nrd1 complex consisting of two RNA-binding proteins Nrd1 and Nab3 and Sen1 helicase. It is established that Nrd1 and Nab3 cooperatively recognize specific termination elements within nascent RNA, GUA[A/G] and UCUU[G], respectively. Interestingly, some transcripts do not require GUA[A/G] motif for transcription termination in vivo and binding in vitro, suggesting the existence of alternative Nrd1-binding motifs. Here we studied the structure and RNA-binding properties of Nrd1 using nuclear magnetic resonance (NMR), fluorescence anisotropy and phenotypic analyses in vivo. We determined the solution structure of a two-domain RNA-binding fragment of Nrd1, formed by an RNA-recognition motif and helix-loop bundle. In Saccharomyces cerevisiae, the Nrd1-dependent termination and processing pathways play an important role in surveillance and processing of non-coding ribonucleic acids (RNAs). The termination and subsequent processing is dependent on the Nrd1 complex consisting of two RNA-binding proteins Nrd1 and Nab3 and Sen1 helicase. It is established that Nrd1 and Nab3 cooperatively recognize specific termination elements within nascent RNA, GUA[A/G] and UCUU[G], respectively. Interestingly, some transcripts do not require GUA[A/G] motif for transcription termination in vivo and binding in vitro, suggesting the existence of alternative Nrd1-binding motifs. Here we studied the structure and RNA-binding properties of Nrd1 using nuclear magnetic resonance (NMR), fluorescence anisotropy and phenotypic analyses in vivo. We determined the solution structure of a two-domain RNA-binding fragment of Nrd1, formed by an RNA-recognition motif and helix-loop bundle.
dcterms:title
Structure and semi-sequence-specific RNA binding of Nrd1 Structure and semi-sequence-specific RNA binding of Nrd1
skos:prefLabel
Structure and semi-sequence-specific RNA binding of Nrd1 Structure and semi-sequence-specific RNA binding of Nrd1
skos:notation
RIV/00216224:14740/14:00073612!RIV15-MSM-14740___
n5:aktivita
n14:P
n5:aktivity
P(ED1.1.00/02.0068), P(EE2.3.20.0042), P(EE2.3.30.0037), P(GBP305/12/G034)
n5:cisloPeriodika
12
n5:dodaniDat
n18:2015
n5:domaciTvurceVysledku
n11:6439608 n11:6897541 n11:1748130 n11:7878788
n5:druhVysledku
n15:J
n5:duvernostUdaju
n16:S
n5:entitaPredkladatele
n10:predkladatel
n5:idSjednocenehoVysledku
47914
n5:idVysledku
RIV/00216224:14740/14:00073612
n5:jazykVysledku
n20:eng
n5:klicovaSlova
protein Nrd1; RNA; untranslated RNA; fluorescence analysis; RNA processing; transcription termination; RNA surveillance; RNA recognition motif
n5:klicoveSlovo
n8:protein%20Nrd1 n8:transcription%20termination n8:RNA n8:RNA%20recognition%20motif n8:fluorescence%20analysis n8:RNA%20surveillance n8:RNA%20processing n8:untranslated%20RNA
n5:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n5:kontrolniKodProRIV
[AE1FDEEF7E79]
n5:nazevZdroje
Nucleic Acids Research
n5:obor
n17:BO
n5:pocetDomacichTvurcuVysledku
4
n5:pocetTvurcuVysledku
4
n5:projekt
n9:GBP305%2F12%2FG034 n9:EE2.3.30.0037 n9:ED1.1.00%2F02.0068 n9:EE2.3.20.0042
n5:rokUplatneniVysledku
n18:2014
n5:svazekPeriodika
42
n5:tvurceVysledku
Pasulka, Josef Bačíková, Veronika Štefl, Richard Kubíček, Karel
n5:wos
000339713200044
s:issn
0305-1048
s:numberOfPages
15
n7:doi
10.1093/nar/gku446
n12:organizacniJednotka
14740