The Department of Biochemistry at the University of Oxford is a centre for world class research and teaching of all aspects of Biochemistry by staff from many different backgrounds and nationalities. Our research addresses a wide range of questions relating to the fundamental basis of all cellular life from man to microbes. This work explains the structures and functions of proteins and nucleic acids, and in doing so addresses the mechanisms of many human diseases. Using this knowledge, other researchers aim to create new vaccines, antiviral and antibacterial therapies to protect and treat humans across the world.
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Professor Mark Sansom, Head of Department
How a group of conserved proteins orchestrate transcription termination in eukaryotes
Figure 1. Homologous CID-containing proteins from budding yeast (S.cerevisiae) and fission yeast (S.pombe) with the conserved regions CID and RRM shown (Click to Enlarge)
A paper published in Nature Communications by Lidia Vasilieva's group in collaboration with researchers at the Division of Structural Biology at the University of Oxford (STRUBI) and the Max-Planck Institute for Biophysical Chemistry in Göttingen, Germany, sheds light on how a group of conserved proteins orchestrate transcription termination in eukaryotes (1).
Unexpectedly, their study also reveals that fission yeast, and possibly other eukaryotes, use a different mechanism from the model eukaryote budding yeast to regulate non-coding transcripts.
Figure 2. The structure of the Seb1 RNA-binding region, solved by X-ray crystallography and to 1.0 Å resolution. The canonical RRM domain is shown in blue and the second domain in green
All steps of transcription - initiation, elongation and termination - are tightly controlled. In eukaryotes, this control is directly coupled to RNA polymerase II (Pol II), a multi-protein complex whose largest subunit has a long C-terminal domain (CTD) with multiple repeats that are conserved across organisms. Many of the residues in the repeat can be reversibly phosphorylated and this is known to regulate key events during the transcription cycle. A conserved group of proteins required for transcription regulation are the CTD readers.
These bind to phosphorylated residues on the CTD, in some cases via a conserved CTD-interacting domain (CID), but it is not fully understood how they mediate CTD function is regulating transcription.