ArticleProceedings of the National Academy of Sciences of the United States of America2005
Fcp1 directly recognizes the C-terminal domain (CTD) and interacts with a site on RNA polymerase II distinct from the CTD.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- CTDP1 governs a Pol II phosphorylation intermediate and coordinates Mediator recruitment, transcription efficiency, and splicing.Nucleic acids research · 2026Article
- Regulation of Skn7-dependent, oxidative stress-induced genes by the RNA polymerase II-CTD phosphatase, Fcp1, and Mediator kinase subunit, Cdk8, in yeast.The Journal of biological chemistry · 2019Article
- Ccr4-Not maintains genomic integrity by controlling the ubiquitylation and degradation of arrested RNAPII.Genes & development · 2019Article
- Biochemical methods to characterize RNA polymerase II elongation complexes.Methods (San Diego, Calif.) · 2019Article
- Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest.The Journal of biological chemistry · 2016Article
- Ccr4-Not and TFIIS Function Cooperatively To Rescue Arrested RNA Polymerase II.Molecular and cellular biology · 2015Article
- Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1.RNA (New York, N.Y.) · 2015Article
- The Ssu72 phosphatase mediates the RNA polymerase II initiation-elongation transition.The Journal of biological chemistry · 2014Article
- The Rpb4/7 module of RNA polymerase II is required for carbon catabolite repressor protein 4-negative on TATA (Ccr4-not) complex to promote elongation.The Journal of biological chemistry · 2014Article
- Greatwall-phosphorylated Endosulfine is both an inhibitor and a substrate of PP2A-B55 heterotrimers.eLife · 2014Article
- RNA polymerase II C-terminal domain: Tethering transcription to transcript and template.Chemical reviews · 2013Review
- A rule-based kinetic model of RNA polymerase II C-terminal domain phosphorylation.Journal of the Royal Society, Interface · 2013Article
- Correct assembly of RNA polymerase II depends on the foot domain and is required for multiple steps of transcription in Saccharomyces cerevisiae.Molecular and cellular biology · 2013Article
- Fcp1 dephosphorylation of the RNA polymerase II C-terminal domain is required for efficient transcription of heat shock genes.Molecular and cellular biology · 2012Article
- RNA polymerase II conserved protein domains as platforms for protein-protein interactions.Transcription · 2011Article
- The multifunctional Ccr4-Not complex directly promotes transcription elongation.Genes & development · 2011Article
- A genome-wide screen for essential yeast genes that affect telomere length maintenance.Nucleic acids research · 2009Article
- The structure of Fcp1, an essential RNA polymerase II CTD phosphatase.Molecular cell · 2008Article
- The protein-phosphatome of the human malaria parasite Plasmodium falciparum.BMC genomics · 2008Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Fcp1 is an essential protein phosphatase that hydrolyzes phosphoserines within the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II). Fcp1 plays a major role in the regulation of CTD phosphorylation and, hence, critically influences the function of Pol II throughout the transcription cycle. The basic understanding of Fcp1-CTD interaction has remained ambiguous because two different modes have been proposed: the "dockingsite" model versus the "distributive" mechanism. Here we demonstrate biochemically that Fcp1 recognizes and dephosphorylates the CTD directly, independent of the globular non-CTD part of the Pol II structure. We point out that the recognition of CTD by the phosphatase is based on random access and is not driven by Pol II conformation. Results from three different types of experiments reveal that the overall interaction between Fcp1 and Pol II is not stable but dynamic. In addition, we show that Fcp1 also interacts with a region on the polymerase distinct from the CTD. We emphasize that this non-CTD site is functionally distinct from the docking site invoked previously as essential for the CTD phosphatase activity of Fcp1. We speculate that Fcp1 interaction with the non-CTD site may mediate its stimulatory effect on transcription elongation reported previously.
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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.