Rtr1 Is a CTD Phosphatase that Regulates RNA Polymerase II during the Transition from Serine 5 to Serine 2 Phosphorylation

Amber L. Mosley, Samantha G. Pattenden, Michael Carey, Swaminathan Venkatesh, Joshua M. Gilmore, Laurence Florens, Jerry L. Workman, Michael P. Washburn

Research output: Contribution to journalArticle

90 Scopus citations

Abstract

Messenger RNA processing is coupled to RNA polymerase II (RNAPII) transcription through coordinated recruitment of accessory proteins to the Rpb1 C-terminal domain (CTD). Dynamic changes in CTD phosphorylation during transcription elongation are responsible for their recruitment, with serine 5 phosphorylation (S5-P) occurring toward the 5′ end of genes and serine 2 phosphorylation (S2-P) occurring toward the 3′ end. The proteins responsible for regulation of the transition state between S5-P and S2-P CTD remain elusive. We show that a conserved protein of unknown function, Rtr1, localizes within coding regions, with maximum levels of enrichment occurring between the peaks of S5-P and S2-P RNAPII. Upon deletion of Rtr1, the S5-P form of RNAPII accumulates in both whole-cell extracts and throughout coding regions; additionally, RNAPII transcription is decreased, and termination defects are observed. Functional characterization of Rtr1 reveals its role as a CTD phosphatase essential for the S5-to-S2-P transition.

Original languageEnglish (US)
Pages (from-to)168-178
Number of pages11
JournalMolecular Cell
Volume34
Issue number2
DOIs
StatePublished - Apr 24 2009

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Keywords

  • DNA
  • PROTEINS

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Mosley, A. L., Pattenden, S. G., Carey, M., Venkatesh, S., Gilmore, J. M., Florens, L., Workman, J. L., & Washburn, M. P. (2009). Rtr1 Is a CTD Phosphatase that Regulates RNA Polymerase II during the Transition from Serine 5 to Serine 2 Phosphorylation. Molecular Cell, 34(2), 168-178. https://doi.org/10.1016/j.molcel.2009.02.025