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Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (NAB) 3 protein
F. Hobor, R. Pergoli, K. Kubicek, D. Hrossova, V. Bacikova, M. Zimmermann, J. Pasulka, C. Hofr, S. Vanacova, R. Stefl
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 2008 to 1 year ago
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from 1905 to 1 year ago
PubMed Central
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- MeSH
- Transcription, Genetic MeSH
- Nuclear Proteins chemistry genetics metabolism MeSH
- Protein Conformation MeSH
- Magnetic Resonance Spectroscopy MeSH
- Protein Multimerization MeSH
- Oligonucleotides chemistry metabolism MeSH
- RNA-Binding Proteins chemistry genetics metabolism MeSH
- Solutions MeSH
- Saccharomyces cerevisiae Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae genetics MeSH
- Base Sequence MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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 β-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. Furthermore, 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 binding to the combined and/or repetitive termination elements elicits efficient termination.
CEITEC Central European Institute of Technology Masaryk University Brno 62500 Czech Republic
National Centre for Biomolecular Research Faculty of Science Masaryk University 62500 Brno Czechia
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