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  Molecular basis for coordinating transcription termination with noncoding RNA degradation.

Tudek, A., Porrua, O., Kabzinski, T., Lidschreiber, M., Kubicek, K., Fortova, A., et al. (2014). Molecular basis for coordinating transcription termination with noncoding RNA degradation. Molecular Cell, 55(3), 467-481. doi:10.1016/j.molcel.2014.05.031.

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Tudek, A., Author
Porrua, O., Author
Kabzinski, T., Author
Lidschreiber, M., Author
Kubicek, K., Author
Fortova, A., Author
Lacroute, F., Author
Vanakova, S., Author
Cramer, P.1, Author           
Stefl, R., Author
Libri, D., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2014-07-242014-08-07
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2014.05.031
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 55 (3) Sequence Number: - Start / End Page: 467 - 481 Identifier: -