The conserved protein Seb1 from fission yeast is recruited to the chromatin during active Pol II transcription

The protein Seb1 from fission yeast contains a conserved CTD-interacting domain (CID) with which it can bind to phosphorylated forms of the Pol II C-terminal domain (CTD) during active transcription. It mainly interacts with Ser2P-CTD but also with Ser5P-CTD. Here, we show the recruitment profile of the protein to chromatin using ChIP-Seq which is mediated mainly via binding to the Pol II-CTD. In addition, it can also interact with nascent RNA via its RNA recognition motif (RRM) domain. Overall design: Two inputs and two immunoprecipitated Seb1-TAP samples were used to perform ChIP-seq. An untagged control (called WT) is also provided.