A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5.

@article{Yeo2003ANR,
  title={A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5.},
  author={Michele Yeo and Patrick P Lin and Michael E Dahmus and Gordon N. Gill},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 28},
  pages={26078-85}
}
The transcription and processing of pre-mRNA in eukaryotic cells are regulated in part by reversible phosphorylation of the C-terminal domain of the largest RNA polymerase (RNAP) II subunit. The CTD phosphatase, FCP1, catalyzes the dephosphorylation of RNAP II and is thought to play a major role in polymerase recycling. This study describes a family of small CTD phosphatases (SCPs) that preferentially catalyze the dephosphorylation of Ser5 within the consensus repeat. The preferred substrate… CONTINUE READING
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