Publication details

Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein

Authors

HÓBOR Fruzsina PERGOLI Roberto KUBÍČEK Karel HROŠŠOVÁ Dominika BAČÍKOVÁ Veronika ZIMMERMANN Michal PASULKA Josef HOFR Ctirad VAŇÁČOVÁ Štěpánka ŠTEFL Richard

Year of publication 2011
Type Article in Periodical
Magazine / Source The Journal of Biological Chemistry
MU Faculty or unit

Central European Institute of Technology

Citation
Doi http://dx.doi.org/10.1074/jbc.M110.158774
Field Biochemistry
Keywords NMR; Protein structure; RNA processing; RNA-protein interaction; Transcription termination
Description 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.
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