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 - PubMed (original) (raw)
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
Cathy B Wilcox et al. Genetics. 2004 May.
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.
Similar articles
- The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae.
Wu X, Rossettini A, Hanes SD. Wu X, et al. Genetics. 2003 Dec;165(4):1687-702. doi: 10.1093/genetics/165.4.1687. Genetics. 2003. PMID: 14704159 Free PMC article. - Functional interaction of the Ess1 prolyl isomerase with components of the RNA polymerase II initiation and termination machineries.
Krishnamurthy S, Ghazy MA, Moore C, Hampsey M. Krishnamurthy S, et al. Mol Cell Biol. 2009 Jun;29(11):2925-34. doi: 10.1128/MCB.01655-08. Epub 2009 Mar 30. Mol Cell Biol. 2009. PMID: 19332564 Free PMC article. - Genetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function.
Wu X, Chang A, Sudol M, Hanes SD. Wu X, et al. Curr Genet. 2001 Dec;40(4):234-42. doi: 10.1007/s00294-001-0257-8. Curr Genet. 2001. PMID: 11795843 - The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.
Hanes SD. Hanes SD. Biochim Biophys Acta. 2014;1839(4):316-33. doi: 10.1016/j.bbagrm.2014.02.001. Epub 2014 Feb 12. Biochim Biophys Acta. 2014. PMID: 24530645 Free PMC article. Review. - The CTD code of RNA polymerase II: a structural view.
Jasnovidova O, Stefl R. Jasnovidova O, et al. Wiley Interdiscip Rev RNA. 2013 Jan-Feb;4(1):1-16. doi: 10.1002/wrna.1138. Epub 2012 Oct 5. Wiley Interdiscip Rev RNA. 2013. PMID: 23042580 Review.
Cited by
- Rct1, a nuclear RNA recognition motif-containing cyclophilin, regulates phosphorylation of the RNA polymerase II C-terminal domain.
Gullerova M, Barta A, Lorkovic ZJ. Gullerova M, et al. Mol Cell Biol. 2007 May;27(10):3601-11. doi: 10.1128/MCB.02187-06. Epub 2007 Mar 5. Mol Cell Biol. 2007. PMID: 17339332 Free PMC article. - Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?
Shaw PE. Shaw PE. EMBO Rep. 2007 Jan;8(1):40-5. doi: 10.1038/sj.embor.7400873. EMBO Rep. 2007. PMID: 17203101 Free PMC article. Review. - Rrd1 isomerizes RNA polymerase II in response to rapamycin.
Jouvet N, Poschmann J, Douville J, Bulet L, Ramotar D. Jouvet N, et al. BMC Mol Biol. 2010 Dec 3;11:92. doi: 10.1186/1471-2199-11-92. BMC Mol Biol. 2010. PMID: 21129186 Free PMC article. - Repeat-Specific Functions for the C-Terminal Domain of RNA Polymerase II in Budding Yeast.
Babokhov M, Mosaheb MM, Baker RW, Fuchs SM. Babokhov M, et al. G3 (Bethesda). 2018 May 4;8(5):1593-1601. doi: 10.1534/g3.118.200086. G3 (Bethesda). 2018. PMID: 29523636 Free PMC article. - Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.
Namitz KEW, Zheng T, Canning AJ, Alicea-Velazquez NL, Castañeda CA, Cosgrove MS, Hanes SD. Namitz KEW, et al. Commun Biol. 2021 Mar 25;4(1):398. doi: 10.1038/s42003-021-01906-8. Commun Biol. 2021. PMID: 33767358 Free PMC article.
References
- FEBS Lett. 1995 May 29;365(2-3):198-202 - PubMed
- Mol Cell Biol. 1995 Jun;15(6):2983-92 - PubMed
- Nature. 1996 Apr 11;380(6574):544-7 - PubMed
- Genetics. 1996 Jun;143(2):661-71 - PubMed
- EMBO J. 1996 Sep 2;15(17):4654-64 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases