5MDT

Structure of the CTD-interacting domain (CID) of Seb1 from S. pombe.

Summary for 5MDT

• Entry DOI: 10.2210/pdb5mdt/pdb
• Descriptor: Rpb7-binding protein seb1 (2 entities in total)
• Functional Keywords: ctd-interacting domain (cid), s. pombe, transcription termination, rna polymerase ii, transcription
• Biological source: Schizosaccharomyces pombe 972h-
• Cellular location: Nucleus : Q9UTE3
• Total number of polymer chains: 1
• Total formula weight: 17911.33

Authors

Wittmann, S.,Renner, M.,Vasiljeva, L.,Grimes, J. (deposition date: 2016-11-13, release date: 2017-04-12, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.62 Å)