Evidence map›Paper›PMID 30135578›Full record

ArticleNature2018

Structure of activated transcription complex Pol II-DSIF-PAF-SPT6.

Seychelle M Vos, Lucas Farnung, Marc Boehning, Christoph Wigge, Andreas Linden, Henning Urlaub, Patrick Cramer

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 287 papers.

0numbers the graph read from it
0cells of the map it votes in
287citing papers in PubMed
17.2field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

287 citing papers in PubMed, 470 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Structural basis for P-TEFb association with BRD4.bioRxiv : the preprint server for biology · 2026
    Article
  5. The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Targeting CDKs in the RNAPII transcription cycle.Nature reviews. Drug discovery · 2026
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Genetic alterations in SUPT6H are associated with neurodevelopmental disorders.Biochimica et biophysica acta. Molecular basis of disease · 2026
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. KAS-CUT&Tag for direct mapping of transcription bubbles.bioRxiv : the preprint server for biology · 2026
    Article
  20. Article

227 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Seychelle M VosMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany.
Lucas FarnungMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany.
Marc BoehningMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany.
Christoph WiggeMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany.
Andreas LindenMax Planck Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry, Göttingen, Germany.
Henning UrlaubMax Planck Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry, Göttingen, Germany.
Patrick CramerMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany. patrick.cramer@mpibpc.mpg.de.
Max Planck Institute for Biophysical Chemistry · DEUniversitätsmedizin Göttingen · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gene regulation involves activation of RNA polymerase II (Pol II) that is paused and bound by the protein complexes DRB sensitivity-inducing factor (DSIF) and negative elongation factor (NELF). Here we show that formation of an activated Pol II elongation complex in vitro requires the kinase function of the positive transcription elongation factor b (P-TEFb) and the elongation factors PAF1 complex (PAF) and SPT6. The cryo-EM structure of an activated elongation complex of Sus scrofa Pol II and Homo sapiens DSIF, PAF and SPT6 was determined at 3.1 Å resolution and compared to the structure of the paused elongation complex formed by Pol II, DSIF and NELF. PAF displaces NELF from the Pol II funnel for pause release. P-TEFb phosphorylates the Pol II linker to the C-terminal domain. SPT6 binds to the phosphorylated C-terminal-domain linker and opens the RNA clamp formed by DSIF. These results provide the molecular basis for Pol II pause release and elongation activation.

Indexed as

Cryoelectron MicroscopyAnimalsDNAHumansModels, MolecularNuclear ProteinsPhosphoproteinsPositive Transcriptional Elongation Factor BRNARNA Polymerase IISus scrofaTranscriptional Elongation FactorsTranscription Elongation, GeneticTranscription FactorsCTR9 protein, humanDNAnegative elongation factorNSMF protein, humanNuclear ProteinsPAF1 protein, humanPhosphoproteinsPositive Transcriptional Elongation Factor BRNARNA Polymerase IISUPT5H protein, humanSUPT6H protein, humanTranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID30135578
OpenAlexW2888537731

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.