ArticleMolecular and cellular biology2007
Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 53 citations in OpenAlex.
- Ssu72: a versatile protein with functions in transcription and beyond.Frontiers in molecular biosciences · 2024Review
- Mammalian Ssu72 phosphatase preferentially considers tissue-specific actively transcribed gene expression by regulating RNA Pol II transcription.Theranostics · 2022Article
- Simplicity is the Ultimate Sophistication-Crosstalk of Post-translational Modifications on the RNA Polymerase II.Journal of molecular biology · 2021Review
- Protein phosphatases in the RNAPII transcription cycle: erasers, sculptors, gatekeepers, and potential drug targets.Genes & development · 2021Review
- Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases.International journal of molecular sciences · 2021Review
- Diverse and conserved roles of the protein Ssu72 in eukaryotes: from yeast to higher organisms.Current genetics · 2021Review
- Review
- RNA polymerase II plays an active role in the formation of gene loops through the Rpb4 subunit.Nucleic acids research · 2019Article
- CPF Recruitment to Non-canonical Transcription Termination Sites Triggers Heterochromatin Assembly and Gene Silencing.Cell reports · 2019Article
- Protein phosphatases of Saccharomyces cerevisiae.Current genetics · 2019Review
- Article
- Context-dependent modulation of Pol II CTD phosphatase SSUP-72 regulates alternative polyadenylation in neuronal development.Genes & development · 2015Article
- Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.ACS chemical biology · 2015Article
- Rpb4/7 facilitates RNA polymerase II CTD dephosphorylation.Nucleic acids research · 2014Article
- The Ssu72 phosphatase mediates the RNA polymerase II initiation-elongation transition.The Journal of biological chemistry · 2014Article
- A gene-specific role for the Ssu72 RNAPII CTD phosphatase in HIV-1 Tat transactivation.Genes & development · 2014Article
- Stress induces changes in the phosphorylation of Trypanosoma cruzi RNA polymerase II, affecting its association with chromatin and RNA processing.Eukaryotic cell · 2014Article
- The interactome of the atypical phosphatase Rtr1 in Saccharomyces cerevisiae.Molecular bioSystems · 2014Article
- CPF-associated phosphatase activity opposes condensin-mediated chromosome condensation.PLoS genetics · 2014Article
- Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA Polymerase II.Molecules (Basel, Switzerland) · 2014Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The RNA polymerase II (RNAP II) transcription cycle is accompanied by changes in the phosphorylation status of the C-terminal domain (CTD), a reiterated heptapeptide sequence (Y(1)S(2)P(3)T(4)S(5)P(6)S(7)) present at the C terminus of the largest RNAP II subunit. One of the enzymes involved in this process is Ssu72, a CTD phosphatase with specificity for serine-5-P. Here we report that the ssu72-2-encoded Ssu72-R129A protein is catalytically impaired in vitro and that the ssu72-2 mutant accumulates the serine-5-P form of RNAP II in vivo. An in vitro transcription system derived from the ssu72-2 mutant exhibits impaired elongation efficiency. Mutations in RPB1 and RPB2, the genes encoding the two largest subunits of RNAP II, were identified as suppressors of ssu72-2. The rpb1-1001 suppressor encodes an R1281A replacement, whereas rpb2-1001 encodes an R983G replacement. This information led us to identify the previously defined rpb2-4 and rpb2-10 alleles, which encode catalytically slow forms of RNAP II, as additional suppressors of ssu72-2. Furthermore, deletion of SPT4, which encodes a subunit of the Spt4-Spt5 early elongation complex, also suppresses ssu72-2, whereas the spt5-242 allele is suppressed by rpb2-1001. These results define Ssu72 as a transcription elongation factor. We propose a model in which Ssu72 catalyzes serine-5-P dephosphorylation subsequent to addition of the 7-methylguanosine cap on pre-mRNA in a manner that facilitates the RNAP II transition into the elongation stage of the transcription cycle.
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