2MOW

Structure of Nrd1p CID - Trf4p NIM complex

2MOW の概要

• エントリーDOI: 10.2210/pdb2mow/pdb
• NMR情報: BMRB: 19954
• 分子名称: Protein NRD1, Poly(A) RNA polymerase protein 2 (2 entities in total)
• 機能のキーワード: transcription termination, rna degradation, rnap ii ctd, protein-protein interaction, transcription
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus (Potential): P53617; Nucleus: P53632
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19732.03

構造登録者

Kabzinski, T.,Stefl, R.,Kubicek, K. (登録日: 2014-05-06, 公開日: 2014-08-13, 最終更新日: 2024-05-15)

主引用文献

Tudek, A.,Porrua, O.,Kabzinski, T.,Lidschreiber, M.,Kubicek, K.,Fortova, A.,Lacroute, F.,Vanacova, S.,Cramer, P.,Stefl, R.,Libri, D.
Molecular Basis for Coordinating Transcription Termination with Noncoding RNA Degradation.
Mol.Cell, 55:467-481, 2014

PubMed 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.

PubMed: 25066235
DOI: 10.1016/j.molcel.2014.05.031

実験手法

SOLUTION NMR