RPRD1A and RPRD1B Are Human RNA Polymerase II C-Terminal Domain Scaffolds for Ser5 Dephosphorylation

@article{Ni2014RPRD1AAR,
  title={RPRD1A and RPRD1B Are Human RNA Polymerase II C-Terminal Domain Scaffolds for Ser5 Dephosphorylation},
  author={Z. Ni and Chao Xu and Xinghua Guo and Gerald O. Hunter and O. Kuznetsova and W. Tempel and E. Marcon and Guoqing Zhong and Hongbo Guo and W. Kuo and Joyce Li and Peter Young and Jonathan B. Olsen and Cuihong Wan and P. Loppnau and Majida El Bakkouri and G. Senisterra and Hao He and H. Huang and S. Sidhu and A. Emili and Shona Murphy and A. Mosley and C. Arrowsmith and J. Min and J. Greenblatt},
  journal={Nature structural \& molecular biology},
  year={2014},
  volume={21},
  pages={686 - 695}
}
The RNA polymerase II (RNAPII) C-terminal domain (CTD) heptapeptide repeats (1-YSPTSPS-7) undergo dynamic phosphorylation and dephosphorylation during the transcription cycle to recruit factors that regulate transcription, RNA processing and chromatin modification. We show here that RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains and interact preferentially via CTD-interaction domains (CIDs) with RNAPII CTD repeats phosphorylated at S2 and S7. Crystal… Expand
Crosstalk between RNA Pol II C-Terminal Domain Acetylation and Phosphorylation via RPRD Proteins.
Crosstalk between RNA Pol II C-Terminal Domain Acetylation and Phosphorylation via RPRD Proteins
Different phosphoisoforms of RNA polymerase II engage the Rtt103 termination factor in a structurally analogous manner
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