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

Basic information
Original title:Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein
Authors:Fruzsina Hóbor, Roberto Pergoli, Karel Kubíček, Dominika Hroššová, Veronika Bačíková, Michal Zimmermann, Josef Pasulka, Ctirad Hofr, Štěpánka Vaňáčová, Richard Štefl
Further information
Citation:HÓBOR, Fruzsina - PERGOLI, Roberto - KUBÍČEK, Karel - HROŠŠOVÁ, Dominika - BAČÍKOVÁ, Veronika - ZIMMERMANN, Michal - PASULKA, Josef - HOFR, Ctirad - VAŇÁČOVÁ, Štěpánka - ŠTEFL, Richard. 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., USA. ISSN 0021-9258, 2011, vol. 286, no. 5, pp. 3645-3657.
Original language:English
Field:Biochemistry
Type:Article in Periodical
Keywords:NMR; Protein structure; RNA processing; RNA-protein interaction; Transcription termination

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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