ArticleGenes & development2014
How an mRNA capping enzyme reads distinct RNA polymerase II and Spt5 CTD phosphorylation codes.
Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 48 citations in OpenAlex.
- Glc7/PP1 triggers Paf1 complex dissociation from RNA polymerase II to enable transcription termination.Genes & development · 2026Article
- YqeK governs the acquisition and removal of nucleoside tetraphosphate caps in Firmicutes.Nucleic acids research · 2026Article
- Glc7/PP1 triggers Paf1 complex dissociation from RNA polymerase II to enable transcription termination.bioRxiv : the preprint server for biology · 2025Article
- DSIF factor Spt5 coordinates transcription, maturation and exoribonucleolysis of RNA polymerase II transcripts.Nature communications · 2025Article
- Structures of co-transcriptional RNA capping enzymes on paused transcription complex.Nature communications · 2024Article
- Transcriptional elongation control in developmental gene expression, aging, and disease.Molecular cell · 2023Review
- Spt5 C-terminal repeat domain phosphorylation and length negatively regulate heterochromatin through distinct mechanisms.PLoS genetics · 2023Article
- PGC-1α senses the CBC of pre-mRNA to dictate the fate of promoter-proximally paused RNAPII.Molecular cell · 2023Article
- Type B and type A influenza polymerases have evolved distinct binding interfaces to recruit the RNA polymerase II CTD.PLoS pathogens · 2022Article
- SPT5 stabilization of promoter-proximal RNA polymerase II.Molecular cell · 2021Article
- PHF3 regulates neuronal gene expression through the Pol II CTD reader domain SPOC.Nature communications · 2021Article
- Simplicity is the Ultimate Sophistication-Crosstalk of Post-translational Modifications on the RNA Polymerase II.Journal of molecular biology · 2021Review
- A novel RNA pol II CTD interaction site on the mRNA capping enzyme is essential for its allosteric activation.Nucleic acids research · 2021Article
- So close, no matter how far: multiple paths connecting transcription to mRNA translation in eukaryotes.EMBO reports · 2020Review
- Spt5 Phosphorylation and the Rtf1 Plus3 Domain Promote Rtf1 Function through Distinct Mechanisms.Molecular and cellular biology · 2020Article
- Interplay of mRNA capping and transcription machineries.Bioscience reports · 2020Review
- Stresses that Raise NpMolecular cell · 2019Article
- Analysis of RNA 5' ends: Phosphate enumeration and cap characterization.Methods (San Diego, Calif.) · 2019Article
- Elongation/Termination Factor Exchange Mediated by PP1 Phosphatase Orchestrates Transcription Termination.Cell reports · 2018Article
- Born to run: control of transcription elongation by RNA polymerase II.Nature reviews. Molecular cell biology · 2018Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Interactions between RNA guanylyltransferase (GTase) and the C-terminal domain (CTD) repeats of RNA polymerase II (Pol2) and elongation factor Spt5 are thought to orchestrate cotranscriptional capping of nascent mRNAs. The crystal structure of a fission yeast GTase•Pol2 CTD complex reveals a unique docking site on the nucleotidyl transferase domain for an 8-amino-acid Pol2 CTD segment, S5PPSYSPTS5P, bracketed by two Ser5-PO4 marks. Analysis of GTase mutations that disrupt the Pol2 CTD interface shows that at least one of the two Ser5-PO4-binding sites is required for cell viability and that each site is important for cell growth at 37°C. Fission yeast GTase binds the Spt5 CTD at a separate docking site in the OB-fold domain that captures the Trp4 residue of the Spt5 nonapeptide repeat T(1)PAW(4)NSGSK. A disruptive mutation in the Spt5 CTD-binding site of GTase is synthetically lethal with mutations in the Pol2 CTD-binding site, signifying that the Spt5 and Pol2 CTDs cooperate to recruit capping enzyme in vivo. CTD phosphorylation has opposite effects on the interaction of GTase with Pol2 (Ser5-PO4 is required for binding) versus Spt5 (Thr1-PO4 inhibits binding). We propose that the state of Thr1 phosphorylation comprises a binary "Spt5 CTD code" that is read by capping enzyme independent of and parallel to its response to the state of the Pol2 CTD.
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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.