ArticleGenetics2004
Genetic interactions with C-terminal domain (CTD) kinases and the CTD of RNA Pol II suggest a role for ESS1 in transcription initiation and elongation in Saccharomyces cerevisiae.
Article in Genetics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.Communications biology · 2021Article
- Repeat-Specific Functions for the C-Terminal Domain of RNA Polymerase II in Budding Yeast.G3 (Bethesda, Md.) · 2018Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- 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
- Role of Ess1 in growth, morphogenetic switching, and RNA polymerase II transcription in Candida albicans.PloS one · 2013Article
- Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle.Molecular and cellular biology · 2012Article
- Understanding and predicting synthetic lethal genetic interactions in Saccharomyces cerevisiae using domain genetic interactions.BMC systems biology · 2011Article
- An investigation of a role for U2 snRNP spliceosomal components in regulating transcription.PloS one · 2011Article
- Updating the CTD Story: From Tail to Epic.Genetics research international · 2011Article
- Rrd1 isomerizes RNA polymerase II in response to rapamycin.BMC molecular biology · 2010Article
- The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway.Molecular cell · 2009Article
- How eukaryotic genes are transcribed.Critical reviews in biochemistry and molecular biology · 2009Review
- Functional interaction of the Ess1 prolyl isomerase with components of the RNA polymerase II initiation and termination machineries.Molecular and cellular biology · 2009Article
- Small family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical research.Perspectives in medicinal chemistry · 2008Article
- Pin1 modulates RNA polymerase II activity during the transcription cycle.Genes & development · 2007Article
- Rct1, a nuclear RNA recognition motif-containing cyclophilin, regulates phosphorylation of the RNA polymerase II C-terminal domain.Molecular and cellular biology · 2007Article
- Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?EMBO reports · 2007Review
- Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires.BMC genomics · 2006Article
- The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.Biochemistry · 2005Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Ess1 is an essential prolyl isomerase that binds the C-terminal domain (CTD) of Rpb1, the large subunit of RNA polymerase II. Ess1 is proposed to control transcription by isomerizing phospho-Ser-Pro peptide bonds within the CTD repeat. To determine which step(s) in the transcription cycle might require Ess1, we examined genetic interactions between ESS1 and genes encoding the known CTD kinases (KIN28, CTK1, BUR1, and SRB10). Although genetic interactions were identified between ESS1 and all four kinases, the clearest interactions were with CTK1 and SRB10. Reduced dosage of CTK1 rescued the growth defect of ess1(ts) mutants, while overexpression of CTK1 enhanced the growth defects of ess1(ts) mutants. Deletion of SRB10 suppressed ess1(ts) and ess1Delta mutants. The interactions suggest that Ess1 opposes the functions of these kinases, which are thought to function in preinitiation and elongation. Using a series of CTD substitution alleles, we also identified Ser5-Pro6 as a potential target for Ess1 isomerization within the first "half" of the CTD repeats. On the basis of the results, we suggest a model in which Ess1-directed conformational changes promote dephosphorylation of Ser5 to stimulate preinitiation complex formation and, later, to inhibit elongation.
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Registered trials
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