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The conserved protein Seb1 drives transcription termination by binding RNA polymerase II and nascent RNA

DOI: 10.1038/ncomms14861 DOI Help

Authors: Sina Wittmann (University of Oxford) , Max Renner (University of Oxford) , Beth R. Watts (University of Oxford) , Oliver Adams (University of Oxford) , Miles Huseyin (University of Oxford) , Carlo Baejen (Max Planck Institute for Biophysical Chemistry) , Kamel El Omari (Diamond Light Source) , Cornelia Kilchert (University of Oxford) , Dong-hyuk Heo (University of Oxford) , Tea Kecman (University of Oxford) , Patrick Cramer (Max Planck Institute for Biophysical Chemistry) , Jonathan Grimes (Wellcome Trust Centre for Human Genetics, University of Oxford; Diamond Light Source) , Lidia Vasiljeva (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: April 2017
Diamond Proposal Number(s): 8423

Open Access Open Access

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.

Journal Keywords: RNA; Transcription; X-ray crystallography

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: B21-High Throughput SAXS , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography


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