| HÓBOR, Fruzsina, Roberto PERGOLI, Karel KUBÍČEK, Dominika HROŠŠOVÁ, Veronika BAČÍKOVÁ, Michal ZIMMERMANN, Josef PASULKA, Ctirad HOFR, Štěpánka VAŇÁČOVÁ and Richard ŠTEFL. Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein. The Journal of Biological Chemistry. Am. Soc. for Biochem. and Mol. Biol., 2011, vol. 286, No 5, p. 3645-3657. ISSN 0021-9258. Available from: https://dx.doi.org/10.1074/jbc.M110.158774. |
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@article{907969,
author = {Hóbor, Fruzsina and Pergoli, Roberto and Kubíček, Karel and Hroššová, Dominika and Bačíková, Veronika and Zimmermann, Michal and Pasulka, Josef and Hofr, Ctirad and Vaňáčová, Štěpánka and Štefl, Richard},
article_number = {5},
doi = {http://dx.doi.org/10.1074/jbc.M110.158774},
keywords = {NMR; Protein structure; RNA processing; RNA-protein interaction; Transcription termination},
language = {eng},
issn = {0021-9258},
journal = {The Journal of Biological Chemistry},
title = {Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein},
volume = {286},
year = {2011}
}
TY - JOUR
ID - 907969
AU - Hóbor, Fruzsina - Pergoli, Roberto - Kubíček, Karel - Hroššová, Dominika - Bačíková, Veronika - Zimmermann, Michal - Pasulka, Josef - Hofr, Ctirad - Vaňáčová, Štěpánka - Štefl, Richard
PY - 2011
TI - Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein
JF - The Journal of Biological Chemistry
VL - 286
IS - 5
SP - 3645-3657
EP - 3645-3657
PB - Am. Soc. for Biochem. and Mol. Biol.
SN - 00219258
KW - NMR
KW - Protein structure
KW - RNA processing
KW - RNA-protein interaction
KW - Transcription termination
N2 - Non-coding RNA polymerase II transcripts are processed by the poly(A) independent termination pathway that requires the Nrd1 complex. The Nrd1 complex includes two RNA-binding proteins, the nuclear polyadenylated RNA-binding (Nab)3 and the nuclear pre-mRNA down-regulation (Nrd)1 that bind their specific termination elements. Here we report the solution structure of the RNA-recognition motif (RRM) of Nab3 in complex with a UCUU oligonucleotide, representing the Nab3 termination element. The structure shows that the first three nucleotides of UCUU are accommodated on the beta-sheet surface of Nab3 RRM, but reveals a sequence specific recognition only for the central cytidine and uridine. The specific contacts we identified are important for binding affinity in vitro as well as for yeast viability. Further, we show that both RNA-binding motifs of Nab3 and Nrd1 alone bind their termination elements with a weak affinity. Interestingly, when Nab3 and Nrd1 form a heterodimer, the affinity to RNA is significantly increased due to the cooperative binding. These findings are in accordance with the model of their function in the poly(A) independent termination, in which the binding to the combined and/or repetitive termination elements elicits efficient termination.
ER -
HÓBOR, Fruzsina, Roberto PERGOLI, Karel KUBÍČEK, Dominika HROŠŠOVÁ, Veronika BAČÍKOVÁ, Michal ZIMMERMANN, Josef PASULKA, Ctirad HOFR, Štěpánka VAŇÁČOVÁ and Richard ŠTEFL. Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein. \textit{The Journal of Biological Chemistry}. Am. Soc. for Biochem. and Mol. Biol., 2011, vol.~286, No~5, p.~3645-3657. ISSN~0021-9258. Available from: https://dx.doi.org/10.1074/jbc.M110.158774.
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