Evidence map›Paper›PMID 30127355›Full record

ArticleNature structural & molecular biology2018

RNA polymerase II clustering through carboxy-terminal domain phase separation.

Marc Boehning, Claire Dugast-Darzacq, Marija Rankovic, Anders S Hansen, Taekyung Yu, Herve Marie-Nelly, David T McSwiggen, Goran Kokic, Gina M Dailey, Patrick Cramer and 2 more

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 360 papers.

0numbers the graph read from it
0cells of the map it votes in
360citing papers in PubMed
31.7field-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

360 citing papers in PubMed, 632 citations in OpenAlex.

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  6. Current Challenges of Transcription Compartmentalization Research.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  15. Review
  16. Review
  17. Article
  18. Residue-level mapping of crowding effects on protein phase separation.Protein science : a publication of the Protein Society · 2026
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 2 countries.

Marc BoehningMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany.ORCID http://orcid.org/0000-0002-4245-5113
Claire Dugast-DarzacqDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
Marija RankovicMax Planck Institute for Biophysical Chemistry, Department of NMR-based Structural Biology, Göttingen, Germany.
Anders S HansenDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
Taekyung YuGerman Center for Neurodegenerative Diseases (DZNE), Göttingen, Germany.
Herve Marie-NellyDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
David T McSwiggenDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
Goran KokicMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany.ORCID http://orcid.org/0000-0001-8912-7099
Gina M DaileyDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
Patrick CramerMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany. Patrick.Cramer@mpibpc.mpg.de.ORCID http://orcid.org/0000-0001-5454-7755
Xavier DarzacqDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA. darzacq@berkeley.edu.
Markus ZweckstetterMax Planck Institute for Biophysical Chemistry, Department of NMR-based Structural Biology, Göttingen, Germany. Markus.Zweckstetter@dzne.de.ORCID http://orcid.org/0000-0002-2536-6581
University of California, Berkeley · USMax Planck Institute for Biophysical Chemistry · DEGerman Center for Neurodegenerative Diseases · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The carboxy-terminal domain (CTD) of RNA polymerase (Pol) II is an intrinsically disordered low-complexity region that is critical for pre-mRNA transcription and processing. The CTD consists of hepta-amino acid repeats varying in number from 52 in humans to 26 in yeast. Here we report that human and yeast CTDs undergo cooperative liquid phase separation, with the shorter yeast CTD forming less-stable droplets. In human cells, truncation of the CTD to the length of the yeast CTD decreases Pol II clustering and chromatin association, whereas CTD extension has the opposite effect. CTD droplets can incorporate intact Pol II and are dissolved by CTD phosphorylation with the transcription initiation factor IIH kinase CDK7. Together with published data, our results suggest that Pol II forms clusters or hubs at active genes through interactions between CTDs and with activators and that CTD phosphorylation liberates Pol II enzymes from hubs for promoter escape and transcription elongation.

Indexed as

Amino Acid SequenceCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesHumansPhosphorylationRepetitive Sequences, Amino AcidRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesRNA Polymerase IISaccharomyces cerevisiae Proteins

Identifiers

PMID30127355
OpenAlexW2887741043

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.