1. Rtr1 Is a CTD Phosphatase that Regulates RNA Polymerase II during the Transition from Serine 5 to Serine 2 Phosphorylation
- Author
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Swaminathan Venkatesh, Laurence Florens, Samantha G. Pattenden, Jerry L. Workman, Amber L. Mosley, Joshua M. Gilmore, Michael P. Washburn, and Michael Carey
- Subjects
Chromatin Immunoprecipitation ,Saccharomyces cerevisiae Proteins ,Transcription, Genetic ,RNA polymerase II ,Saccharomyces cerevisiae ,Biology ,environment and public health ,Article ,Serine ,03 medical and health sciences ,Open Reading Frames ,Transcription (biology) ,Protein Interaction Mapping ,Phosphoprotein Phosphatases ,Phosphorylation ,Transcription factor ,RNA polymerase II holoenzyme ,Molecular Biology ,030304 developmental biology ,0303 health sciences ,Messenger RNA ,Models, Genetic ,030302 biochemistry & molecular biology ,Cell Biology ,Molecular biology ,Proton-Translocating ATPases ,biology.protein ,RNA Polymerase II ,Transcription factor II D ,Transcription Factors - 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 towards the 5’ end of genes and serine 2 phosphorylation (S2-P) occurring towards 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.
- Published
- 2009
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