ArticleGenetics2003
The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae.
Article in Genetics, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 55 citations in OpenAlex.
- Domain acquisition enabled functional expansion of the TFIIS transcription factor family.Cell & bioscience · 2025Review
- ZmELP1, an Elongator complex subunit, is required for the maintenance of histone acetylation and RNA Pol II phosphorylation in maize kernels.Plant biotechnology journal · 2024Article
- A crucial role for dynamic expression of components encoding the negative arm of the circadian clock.Nature communications · 2023Article
- Diverse and dynamic forms of gene regulation by the S. cerevisiae histone methyltransferase Set1.Current genetics · 2023Review
- SPOC domain proteins in health and disease.Genes & development · 2023Review
- An integrated SAGA and TFIID PIC assembly pathway selective for poised and induced promoters.Genes & development · 2022Article
- PHF3 regulates neuronal gene expression through the Pol II CTD reader domain SPOC.Nature communications · 2021Article
- Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.Communications biology · 2021Article
- Interrogation of the cell wall integrity pathway inGene: X · 2020Article
- Elongator Is Required for Root Stem Cell Maintenance by RegulatingPlant physiology · 2019Article
- Subgenic Pol II interactomes identify region-specific transcription elongation regulators.Molecular systems biology · 2017Article
- Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.ACS chemical biology · 2015Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- Termination of Transcription of Short Noncoding RNAs by RNA Polymerase II.Annual review of biochemistry · 2015Review
- Rrd1p, an RNA polymerase II-specific prolyl isomerase and activator of phosphoprotein phosphatase, promotes transcription independently of rapamycin response.Nucleic acids research · 2014Article
- The yeast Ess1 prolyl isomerase controls Swi6 and Whi5 nuclear localization.G3 (Bethesda, Md.) · 2014Article
- The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Biochimica et biophysica acta · 2014Review
- PHD and TFIIS-Like domains of the Bye1 transcription factor determine its multivalent genomic distribution.PloS one · 2014Article
- Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5.Nature structural & molecular biology · 2013Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Transcription by RNA polymerase II (pol II) requires the ordered binding of distinct protein complexes to catalyze initiation, elongation, termination, and coupled mRNA processing events. One or more proteins from each complex are known to bind pol II via the carboxy-terminal domain (CTD) of the largest subunit, Rpb1. How binding is coordinated is not known, but it might involve conformational changes in the CTD induced by the Ess1 peptidyl-prolyl cis/trans isomerase. Here, we examined the role of ESS1 in transcription by studying one of its multicopy suppressors, BYE1. We found that Bye1 is a negative regulator of transcription elongation. This led to the finding that Ess1 also inhibits elongation; Ess1 opposes elongation factors Dst1 and Spt4/5, and overexpression of ESS1 makes cells more sensitive to the elongation inhibitor 6-AU. In reporter gene assays, ess1 mutations reduce the ability of elongation-arrest sites to stall polymerase. We also show that Ess1 acts positively in transcription termination, independent of its role in elongation. We propose that Ess1-induced conformational changes attenuate pol II elongation and help coordinate the ordered assembly of protein complexes on the CTD. In this way, Ess1 might regulate the transition between multiple steps of transcription.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.