ArticleProceedings of the National Academy of Sciences of the United States of America1997
An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
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Who cites it
59 citing papers in PubMed, 145 citations in OpenAlex.
- Cell Cycle-Dependent Transcription: The Cyclin Dependent Kinase Cdk1 Is a Direct Regulator of Basal Transcription Machineries.International journal of molecular sciences · 2022Review
- Targeting transcription cycles in cancer.Nature reviews. Cancer · 2022Review
- Oxidative stress induces Ser 2 dephosphorylation of the RNA polymerase II CTD and premature transcription termination.Transcription · 2021Article
- Protein phosphatases in the RNAPII transcription cycle: erasers, sculptors, gatekeepers, and potential drug targets.Genes & development · 2021Review
- Regulation of the Ras-Related Signaling Pathway by Small Molecules Containing an Indole Core Scaffold: A Potential Antitumor Therapy.Frontiers in pharmacology · 2020Review
- 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
- Regulation of Androgen Receptor Activity by Transient Interactions of Its Transactivation Domain with General Transcription Regulators.Structure (London, England : 1993) · 2018Article
- Identification of Novel Biomarkers for Behcet Disease Diagnosis Using Human Proteome Microarray Approach.Molecular & cellular proteomics : MCP · 2017Article
- Dephosphorylating eukaryotic RNA polymerase II.Biochimica et biophysica acta · 2016Review
- Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1.RNA (New York, N.Y.) · 2015Article
- Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
- The interactome of the atypical phosphatase Rtr1 in Saccharomyces cerevisiae.Molecular bioSystems · 2014Article
- Rat1p maintains RNA polymerase II CTD phosphorylation balance.RNA (New York, N.Y.) · 2014Article
- Global analysis of serine/threonine and tyrosine protein phosphatase catalytic subunit genes in Neurospora crassa reveals interplay between phosphatases and the p38 mitogen-activated protein kinase.G3 (Bethesda, Md.) · 2014Article
- RNA polymerase II C-terminal domain: Tethering transcription to transcript and template.Chemical reviews · 2013Review
- Viewing serine/threonine protein phosphatases through the eyes of drug designers.The FEBS journal · 2013Review
- The RNA polymerase II CTD coordinates transcription and RNA processing.Genes & development · 2012Review
- Emerging Views on the CTD Code.Genetics research international · 2012Article
- Cell cycle regulators interact with pathways that modulate microtubule stability in Saccharomyces cerevisiae.Eukaryotic cell · 2011Article
- UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the essential components of a phosphatase that specifically dephosphorylates the Saccharomyces cerevisiae RNA polymerase II (RPII) large subunit C-terminal domain (CTD) is a novel polypeptide encoded by an essential gene termed FCP1. The Fcp1 protein is localized to the nucleus, and it binds the largest subunit of the yeast general transcription factor IIF (Tfg1). In vitro, transcription factor IIF stimulates phosphatase activity in the presence of Fcp1 and a second complementing fraction. Two distinct regions of Fcp1 are capable of binding to Tfg1, but the C-terminal Tfg1 binding domain is dispensable for activity in vivo and in vitro. Sequence comparison reveals that residues 173-357 of Fcp1 correspond to an amino acid motif present in proteins of unknown function predicted in many organisms.
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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.