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Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination.

The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) serves an important role in coordinating stage-specific recruitment and release of cellular machines during transcription. Dynamic placement and removal of phosphorylation marks on different residues of a repeating heptapeptide (YSPTSPS) of the CTD underlies the engagement of relevant cellular machinery. Whereas sequential placement of phosphorylation marks is well explored, genome-wide engagement of phosphatases that remove these CTD marks is poorly understood. In particular, identifying the enzyme that erases phospho-Ser7 (Ser7-P) marks is especially important, because we find that substituting this residue with a glutamate, a phospho-mimic, is lethal. Our observations implicate Ssu72 as a Ser7-P phosphatase. We report that removal of all phospho-CTD marks during transcription termination is mechanistically coupled. An inability to remove these marks prevents Pol II from terminating efficiently and will likely impede subsequent assembly into the pre-initiation complex.

Pubmed ID: 22235117

Authors

  • Zhang DW
  • Mosley AL
  • Ramisetty SR
  • Rodríguez-Molina JB
  • Washburn MP
  • Ansari AZ

Journal

The Journal of biological chemistry

Publication Data

March 9, 2012

Associated Grants

  • Agency: NHGRI NIH HHS, Id: 5T32HG002760

Mesh Terms

  • Amino Acid Motifs
  • Amino Acid Substitution
  • Mutation, Missense
  • Phosphoprotein Phosphatases
  • Protein Structure, Tertiary
  • RNA Polymerase II
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Serine
  • Transcription, Genetic
  • mRNA Cleavage and Polyadenylation Factors