ArticleProceedings of the National Academy of Sciences of the United States of America2003
Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 48 citations in OpenAlex.
- CTDP1 and RPB7 stabilize Pol II and permit reinitiation.Nature communications · 2025Article
- A glutamine-based single α-helix scaffold to target globular proteins.Nature communications · 2022Article
- Cyclin-Dependent Kinases (CDK) and Their Role in Diseases Development-Review.International journal of molecular sciences · 2021Review
- Structure and mechanism of the RNA polymerase II transcription machinery.Genes & development · 2020Review
- Regulation of Androgen Receptor Activity by Transient Interactions of Its Transactivation Domain with General Transcription Regulators.Structure (London, England : 1993) · 2018Article
- 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
- Position of the general transcription factor TFIIF within the RNA polymerase II transcription preinitiation complex.The EMBO journal · 2010Article
- The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction.The Journal of biological chemistry · 2010Article
- Structure and mechanism of the RNA polymerase II transcription machinery.Nature structural & molecular biology · 2004Review
- NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
After mRNA transcription termination in eukaryotes, the hyperphosphorylated form of RNA polymerase II (pol II0) must be recycled by TFIIF-associating C-terminal domain phosphatase (FCP1), the phosphatase responsible for dephosphorylating the C-terminal domain of the largest polymerase subunit. Transcription factor (TF)-IIF stimulates the activity of FCP1, and the RNA polymerase II-associating protein 74 subunit of TFIIF forms a complex with FCP1 in both human and yeast. Here, we report a cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1 (residues 944-961). These results illustrate the molecular mechanism by which TFIIF efficiently recruits FCP1 to the pol II transcription machinery for recycling of the polymerase.
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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.