5MDU

Structure of the RNA recognition motif (RRM) of Seb1 from S. pombe.

5MDU の概要

• エントリーDOI: 10.2210/pdb5mdu/pdb
• 関連するPDBエントリー: 5MDT
• 分子名称: Rpb7-binding protein seb1, CHLORIDE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: rna recognition motif (rrm), s. pombe, transcription termination, rna binding, transcription
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• 細胞内の位置: Nucleus : Q9UTE3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17643.45

構造登録者

Wittmann, S.,Renner, M.,El Omari, K.,Adams, O.,Vasiljeva, L.,Grimes, J. (登録日: 2016-11-13, 公開日: 2017-04-12, 最終更新日: 2024-05-08)

主引用文献

Wittmann, S.,Renner, M.,Watts, B.R.,Adams, O.,Huseyin, M.,Baejen, C.,El Omari, K.,Kilchert, C.,Heo, D.H.,Kecman, T.,Cramer, P.,Grimes, J.M.,Vasiljeva, L.
The conserved protein Seb1 drives transcription termination by binding RNA polymerase II and nascent RNA.
Nat Commun, 8:14861-14861, 2017

PubMed Abstract: Termination of RNA polymerase II (Pol II) transcription is an important step in the transcription cycle, which involves the dislodgement of polymerase from DNA, leading to release of a functional transcript. Recent studies have identified the key players required for this process and showed that a common feature of these proteins is a conserved domain that interacts with the phosphorylated C-terminus of Pol II (CTD-interacting domain, CID). However, the mechanism by which transcription termination is achieved is not understood. Using genome-wide methods, here we show that the fission yeast CID-protein Seb1 is essential for termination of protein-coding and non-coding genes through interaction with S2-phosphorylated Pol II and nascent RNA. Furthermore, we present the crystal structures of the Seb1 CTD- and RNA-binding modules. Unexpectedly, the latter reveals an intertwined two-domain arrangement of a canonical RRM and second domain. These results provide important insights into the mechanism underlying eukaryotic transcription termination.

PubMed: 28367989
DOI: 10.1038/ncomms14861

実験手法

X-RAY DIFFRACTION (1.02 Å)