ArticleScience (New York, N.Y.)2011
RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3' end processing.
Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
94 citing papers in PubMed.
- Communication is key: combinatorial phosphorylation and functional cross-talk in the RNA polymerase II CTD code.Biochemical Society transactions · 2026Review
- Live-cell single-molecule dynamics of eukaryotic RNA polymerase machineries.Science (New York, N.Y.) · 2026Article
- FeaSion decodes the regulatory landscape and functional diversity of RNA polymerase II CTD phosphorylation.Science advances · 2025Article
- RNA polymerase II transcription compartments - from factories to condensates.Nature reviews. Genetics · 2025Review
- Tripartite phosphorylation of SPT5 by CDK9 times pause release and tunes elongation rate of RNA polymerase II.Molecular cell · 2025Article
- Cyclin-dependent protein kinases and cell cycle regulation in biology and disease.Signal transduction and targeted therapy · 2025Review
- Defining gene ends: RNA polymerase II CTD threonine 4 phosphorylation marks transcription termination regions genome-wide.Nucleic acids research · 2025Article
- Unmasking a hidden code during transcription: A practical strategy to reveal Thr4 phosphorylation in RNA polymerase II.Methods in enzymology · 2025Article
- Herpes simplex virus 1 inhibits phosphorylation of RNA polymerase II CTD serine-7.Journal of virology · 2024Article
- Disordered C-terminal domain drives spatiotemporal confinement of RNAPII to enhance search for chromatin targets.Nature cell biology · 2024Article
- Disordered C-terminal domain drives spatiotemporal confinement of RNAPII to enhance search for chromatin targets.bioRxiv : the preprint server for biology · 2023Article
- Regulation of mature mRNA levels by RNA processing efficiency.NAR genomics and bioinformatics · 2023Article
- Knowing when to stop: Transcription termination on protein-coding genes by eukaryotic RNAPII.Molecular cell · 2023Review
- Transcription associated cyclin-dependent kinases as therapeutic targets for prostate cancer.Oncogene · 2022Review
- Mammalian Ssu72 phosphatase preferentially considers tissue-specific actively transcribed gene expression by regulating RNA Pol II transcription.Theranostics · 2022Article
- Oxidative stress induces Ser 2 dephosphorylation of the RNA polymerase II CTD and premature transcription termination.Transcription · 2021Article
- CREPT serves as a biomarker of poor survival in pancreatic ductal adenocarcinoma.Cellular oncology (Dordrecht, Netherlands) · 2021Article
- Article
- Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021Review
- CDK11 is required for transcription of replication-dependent histone genes.Nature structural & molecular biology · 2020Article
34 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The RNA polymerase II (RNAP II) largest subunit contains a C-terminal domain (CTD) with up to 52 Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7) consensus repeats. Serines 2, 5, and 7 are known to be phosphorylated, and these modifications help to orchestrate the interplay between transcription and processing of messenger RNA (mRNA) precursors. Here, we provide evidence that phosphorylation of CTD Thr(4) residues is required specifically for histone mRNA 3' end processing, functioning to facilitate recruitment of 3' processing factors to histone genes. Like Ser(2), Thr(4) phosphorylation requires the CTD kinase CDK9 and is evolutionarily conserved from yeast to human. Our data thus illustrate how a CTD modification can play a highly specific role in facilitating efficient gene expression.
Indexed as
Identifiers
What OpenQuestion holds
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.