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@article{1182096,
author = {Bačíková, Veronika and Pasulka, Josef and Kubíček, Karel and Štefl, Richard},
article_location = {United Kingdom},
article_number = {12},
doi = {http://dx.doi.org/10.1093/nar/gku446},
keywords = {protein Nrd1; RNA; untranslated RNA; fluorescence analysis; RNA processing; transcription termination; RNA surveillance; RNA recognition motif},
language = {eng},
issn = {0305-1048},
journal = {Nucleic Acids Research},
title = {Structure and semi-sequence-specific RNA binding of Nrd1},
url = {http://nar.oxfordjournals.org/content/early/2014/05/23/nar.gku446.long},
volume = {42},
year = {2014}
}
TY - JOUR
ID - 1182096
AU - Bačíková, Veronika - Pasulka, Josef - Kubíček, Karel - Štefl, Richard
PY - 2014
TI - Structure and semi-sequence-specific RNA binding of Nrd1
JF - Nucleic Acids Research
VL - 42
IS - 12
SP - 8024-8038
EP - 8024-8038
PB - Oxford University Press
SN - 03051048
KW - protein Nrd1
KW - RNA
KW - untranslated RNA
KW - fluorescence analysis
KW - RNA processing
KW - transcription termination
KW - RNA surveillance
KW - RNA recognition motif
UR - http://nar.oxfordjournals.org/content/early/2014/05/23/nar.gku446.long
L2 - http://nar.oxfordjournals.org/content/early/2014/05/23/nar.gku446.long
N2 - 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. NMR and fluorescence data show that not only GUA[A/G] but also several other G-rich and AU-rich motifs are able to bind Nrd1 with affinity in a low micromolar range. The broad substrate specificity is achieved by adaptable interaction surfaces of the RNA-recognition motif and helix-loop bundle domains that sandwich the RNA substrates. Our findings have implication for the role of Nrd1 in termination and processing of many non-coding RNAs arising from bidirectional pervasive transcription. © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research
ER -
BAČÍKOVÁ, Veronika, Josef PASULKA, Karel KUBÍČEK a Richard ŠTEFL. Structure and semi-sequence-specific RNA binding of Nrd1. \textit{Nucleic Acids Research}. United Kingdom: Oxford University Press, 2014, roč.~42, č.~12, s.~8024-8038. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gku446.
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