ArticleRNA (New York, N.Y.)2015
Fission yeast RNA triphosphatase reads an Spt5 CTD code.
Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- DSIF factor Spt5 coordinates transcription, maturation and exoribonucleolysis of RNA polymerase II transcripts.Nature communications · 2025Article
- The CDK9-SPT5 Axis in Control of Transcription Elongation by RNAPII.Journal of molecular biology · 2025Review
- Structures of co-transcriptional RNA capping enzymes on paused transcription complex.Nature communications · 2024Article
- Structural advances in transcription elongation.Current opinion in structural biology · 2022Review
- Interplay of mRNA capping and transcription machineries.Bioscience reports · 2020Review
- Elongation/Termination Factor Exchange Mediated by PP1 Phosphatase Orchestrates Transcription Termination.Cell reports · 2018Article
- Spt5 Plays Vital Roles in the Control of Sense and Antisense Transcription Elongation.Molecular cell · 2017Article
- Article
- Functional interaction of Rpb1 and Spt5 C-terminal domains in co-transcriptional histone modification.Nucleic acids research · 2015Article
- THZ1 Reveals Roles for Cdk7 in Co-transcriptional Capping and Pausing.Molecular cell · 2015Article
- Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1.RNA (New York, N.Y.) · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
mRNA capping enzymes are directed to nascent RNA polymerase II (Pol2) transcripts via interactions with the carboxy-terminal domains (CTDs) of Pol2 and transcription elongation factor Spt5. Fission yeast RNA triphosphatase binds to the Spt5 CTD, comprising a tandem repeat of nonapeptide motif TPAWNSGSK. Here we report the crystal structure of a Pct1·Spt5-CTD complex, which revealed two CTD docking sites on the Pct1 homodimer that engage TPAWN segments of the motif. Each Spt5 CTD interface, composed of elements from both subunits of the homodimer, is dominated by van der Waals contacts from Pct1 to the tryptophan of the CTD. The bound CTD adopts a distinctive conformation in which the peptide backbone makes a tight U-turn so that the proline stacks over the tryptophan. We show that Pct1 binding to Spt5 CTD is antagonized by threonine phosphorylation. Our results fortify an emerging concept of an "Spt5 CTD code" in which (i) the Spt5 CTD is structurally plastic and can adopt different conformations that are templated by particular cellular Spt5 CTD receptor proteins; and (ii) threonine phosphorylation of the Spt5 CTD repeat inscribes a binary on-off switch that is read by diverse CTD receptors, each in its own distinctive manner.
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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.