ArticleMolecular and cellular biology2009
Functional interaction of the Ess1 prolyl isomerase with components of the RNA polymerase II initiation and termination machineries.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- Domain acquisition enabled functional expansion of the TFIIS transcription factor family.Cell & bioscience · 2025Review
- RNA Pol II Assembly Affects ncRNA Expression.International journal of molecular sciences · 2023Article
- SPOC domain proteins in health and disease.Genes & development · 2023Review
- 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
- Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.Communications biology · 2021Article
- RNA polymerase II phosphorylation and gene looping: new roles for the Rpb4/7 heterodimer in regulating gene expression.Current genetics · 2020Review
- Genetic interactions and transcriptomics implicate fission yeast CTD prolyl isomerase Pin1 as an agent of RNA 3' processing and transcription termination that functions via its effects on CTD phosphatase Ssu72.Nucleic acids research · 2020Article
- Tissue-specific regulation of alternative polyadenylation represses expression of a neuronal ankyrin isoform inDevelopment (Cambridge, England) · 2017Article
- Subgenic Pol II interactomes identify region-specific transcription elongation regulators.Molecular systems biology · 2017Article
- A Conserved Nuclear Cyclophilin Is Required for Both RNA Polymerase II Elongation and Co-transcriptional Splicing in Caenorhabditis elegans.PLoS genetics · 2016Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.Biomolecules · 2015Review
- Human DNA-binding peptidyl-prolyl cis/trans isomerase Par14 is cell cycle dependently expressed and associates with chromatin in vivo.BMC biochemistry · 2015Article
- Rpb4/7 facilitates RNA polymerase II CTD dephosphorylation.Nucleic acids research · 2014Article
- The yeast Ess1 prolyl isomerase controls Swi6 and Whi5 nuclear localization.G3 (Bethesda, Md.) · 2014Article
- Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA Polymerase II.Molecules (Basel, Switzerland) · 2014Review
- PHD and TFIIS-Like domains of the Bye1 transcription factor determine its multivalent genomic distribution.PloS one · 2014Article
- The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Biochimica et biophysica acta · 2014Review
- RNA polymerase II C-terminal domain: Tethering transcription to transcript and template.Chemical reviews · 2013Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) is a reiterated heptad sequence (Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7) that plays a key role in the transcription cycle, coordinating the exchange of transcription and RNA processing factors. The structure of the CTD is flexible and undergoes conformational changes in response to serine phosphorylation and proline isomerization. Here we report that the Ess1 peptidyl prolyl isomerase functionally interacts with the transcription initiation factor TFIIB and with the Ssu72 CTD phosphatase and Pta1 components of the CPF 3'-end processing complex. The ess1(A144T) and ess1(H164R) mutants, initially described by Hanes and coworkers (Yeast 5:55-72, 1989), accumulate the pSer5 phosphorylated form of Pol II; confer phosphate, galactose, and inositol auxotrophies; and fail to activate PHO5, GAL10, and INO1 reporter genes. These mutants are also defective for transcription termination, but in vitro experiments indicate that this defect is not caused by altering the processing efficiency of the cleavage/polyadenylation machinery. Consistent with a role in initiation and termination, Ess1 associates with the promoter and terminator regions of the PMA1 and PHO5 genes. We propose that Ess1 facilitates pSer5-Pro6 dephosphorylation by generating the CTD structural conformation recognized by the Ssu72 phosphatase and that pSer5 dephosphorylation affects both early and late stages of the transcription cycle.
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