title: RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7.
abstract: At the 3' ends of protein-coding genes, RNA polymerase (Pol) II is dephosphorylated at tyrosine residues (Tyr1) of its C-terminal domain (CTD). In addition, the associated cleavage-and-polyadenylation factor (CPF) cleaves the transcript and adds a poly(a) tail. Whether these events are coordinated and how they lead to transcription termination remains poorly understood. Here we show that CPF from Saccharomyces cerevisiae is a Pol II-CTD phosphatase and that the CPF subunit Glc7 dephosphorylates Tyr1 in vitro. In vivo, the activity of Glc7 is required for normal Tyr1 dephosphorylation at the polyadenylation site, for recruitment of termination factors Pcf11 and Rtt103 and for normal Pol II termination. These results show that transcription termination involves Tyr1 dephosphorylation of the CTD and indicate that pre-mRNA processing by CPF and transcription termination are coupled via Glc7-dependent Pol II-Tyr1 dephosphorylation.
authors.affiliation: Gene Center Munich and Department of Biochemistry, Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Munich, Germany.
authors.forename: Amelie
authors.initials: A
authors.lastname: Schreieck
authors.affiliation: Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, United Kingdom.
authors.forename: Ashley D
authors.initials: AD
authors.lastname: Easter
authors.affiliation: Gene Center Munich and Department of Biochemistry, Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Munich, Germany.
authors.forename: Stefanie
authors.initials: S
authors.lastname: Etzold
authors.affiliation: Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, United Kingdom.
authors.forename: Katrin
authors.initials: K
authors.lastname: Wiederhold
authors.affiliation: Gene Center Munich and Department of Biochemistry, Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Munich, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Lidschreiber
authors.affiliation: Gene Center Munich and Department of Biochemistry, Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Munich, Germany.
authors.forename: Patrick
authors.initials: P
authors.lastname: Cramer
authors.affiliation: Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, United Kingdom.
authors.forename: Lori A
authors.initials: LA
authors.lastname: Passmore
mesh_terms: D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D010766:Phosphorylation; D054645:Protein Phosphatase 1 / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D012319:RNA Polymerase II / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D061806:Transcription Termination, Genetic; D014443:Tyrosine / Q000378:metabolism*; D039221:mRNA Cleavage and Polyadenylation Factors / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
chemical_list: D021122:Protein Subunits; C416934:SSU72 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D039221:mRNA Cleavage and Polyadenylation Factors; D014443:Tyrosine; D012319:RNA Polymerase II; C092048:GLC7 protein, S cerevisiae; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1