Evidence map›Paper›PMID 34887565›Full record

ArticleNature structural & molecular biology2021

Cryo-EM structures of human RNA polymerase I.

Agata D Misiaszek, Mathias Girbig, Helga Grötsch, Florence Baudin, Brice Murciano, Aleix Lafita, Christoph W Müller

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 50 citations in OpenAlex.

  1. Resolving Sub-Nuclear Architecture from Compartments to Functional Domains.International journal of molecular sciences · 2026
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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

7 authors at 3 institutions in 2 countries.

Agata D MisiaszekStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0002-9763-1815
Mathias GirbigStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0003-3442-5448
Helga GrötschStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Florence BaudinStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0003-0816-0861
Brice MurcianoStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0001-8886-2972
Aleix LafitaEuropean Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Cambridge, UK.ORCID http://orcid.org/0000-0003-1549-3162
Christoph W MüllerStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. christoph.mueller@embl.de.ORCID http://orcid.org/0000-0003-2176-8337
European Molecular Biology Laboratory · DEEuropean Molecular Biology Organization · DEEuropean Bioinformatics Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA polymerase I (Pol I) specifically synthesizes ribosomal RNA. Pol I upregulation is linked to cancer, while mutations in the Pol I machinery lead to developmental disorders. Here we report the cryo-EM structure of elongating human Pol I at 2.7 Å resolution. In the exit tunnel, we observe a double-stranded RNA helix that may support Pol I processivity. Our structure confirms that human Pol I consists of 13 subunits with only one subunit forming the Pol I stalk. Additionally, the structure of human Pol I in complex with the initiation factor RRN3 at 3.1 Å resolution reveals stalk flipping upon RRN3 binding. We also observe an inactivated state of human Pol I bound to an open DNA scaffold at 3.3 Å resolution. Lastly, the high-resolution structure of human Pol I allows mapping of disease-related mutations that can aid understanding of disease etiology.

Indexed as

Binding SitesCryoelectron MicroscopyDNA-Binding ProteinsHumansModels, MolecularNeoplasmsPol1 Transcription Initiation Complex ProteinsProtein BindingProtein ConformationProtein MultimerizationRNA Polymerase IRNA, RibosomalTranscription, GeneticDNA-Binding ProteinsPol1 Transcription Initiation Complex ProteinsRNA Polymerase IRNA, RibosomalRRN3 protein, human

Identifiers

PMID34887565
PMCPMC8660638
OpenAlexW4205339332

What OpenQuestion holds

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LicenceCC BY
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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.