title: Rtr1 is a CTD phosphatase that regulates RNA polymerase II during the transition from serine 5 to serine 2 phosphorylation.
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.
authors.affiliation: Stowers Institute for Medical Research, Kansas City, MO 64110, USA.
authors.forename: Amber L
authors.initials: AL
authors.lastname: Mosley
authors.forename: Samantha G
authors.initials: SG
authors.lastname: Pattenden
authors.forename: Michael
authors.initials: M
authors.lastname: Carey
authors.forename: Swaminathan
authors.initials: S
authors.lastname: Venkatesh
authors.forename: Joshua M
authors.initials: JM
authors.lastname: Gilmore
authors.forename: Laurence
authors.initials: L
authors.lastname: Florens
authors.forename: Jerry L
authors.initials: JL
authors.lastname: Workman
authors.forename: Michael P
authors.initials: MP
authors.lastname: Washburn
mesh_terms: D047369:Chromatin Immunoprecipitation; D008957:Models, Genetic; D016366:Open Reading Frames; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D010766:Phosphorylation; D025941:Protein Interaction Mapping; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012319:RNA Polymerase II / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D012694:Serine / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D014158:Transcription, Genetic
chemical_list: C530135:Rtr1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D012694:Serine; D012319:RNA Polymerase II; D010749:Phosphoprotein Phosphatases; C116022:carboxy-terminal domain phosphatase; C092477:PMA1 protein, S cerevisiae; D006180:Proton-Translocating ATPases