The Nrd1-Nab3-Sen1 (NNS) complex is essential for controlling pervasive transcription and generating sn/snoRNAs in S. cerevisiae. The NNS complex terminates transcription of noncoding RNA genes and promotes exosome-dependent processing/degradation of the released transcripts. The Trf4-Air2-Mtr4 (TRAMP) complex polyadenylates NNS target RNAs and favors their degradation. NNS-dependent termination and degradation are coupled, but the mechanism underlying this coupling remains enigmatic. Here we provide structural and functional evidence demonstrating that the same domain of Nrd1p interacts with RNA polymerase II and Trf4p in a mutually exclusive manner, thus defining two alternative forms of the NNS complex, one involved in termination and the other in degradation. We show that the Nrd1-Trf4 interaction is required for optimal exosome activity in vivo and for the stimulation of polyadenylation of NNS targets by TRAMP in vitro. We propose that transcription termination and RNA degradation are coordinated by switching between two alternative partners of the NNS complex.
- MeSH
- DNA-dependentní DNA-polymerasy chemie metabolismus MeSH
- exozómy metabolismus MeSH
- fungální RNA metabolismus MeSH
- konformace nukleové kyseliny MeSH
- magnetická rezonanční spektroskopie MeSH
- molekulární modely MeSH
- nekódující RNA metabolismus MeSH
- polyadenylace MeSH
- proteiny vázající RNA chemie metabolismus MeSH
- RNA-polymerasa II metabolismus MeSH
- Saccharomyces cerevisiae - proteiny chemie metabolismus MeSH
- Saccharomyces cerevisiae genetika MeSH
- stabilita RNA MeSH
- terminace genetické transkripce * MeSH
- vazebná místa MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
