Evidence map›Paper›PMID 32066962›Full record

ArticleNature structural & molecular biology2020

Structural basis for RNA polymerase III transcription repression by Maf1.

Matthias K Vorländer, Florence Baudin, Robyn D Moir, René Wetzel, Wim J H Hagen, Ian M Willis, Christoph W Müller

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

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  15. RNA Polymerases I and III in development and disease.Seminars in cell & developmental biology · 2023
    Review
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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.

Matthias K VorländerStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Florence BaudinStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Robyn D MoirDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA.
René WetzelStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Wim J H HagenStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0001-6229-2692
Ian M WillisDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA.
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 · DEAlbert Einstein College of Medicine · USHeidelberg University · DE

Funding

MAF1 Function and Metabolic InefficiencyR01GM120358 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI WILLIS, IAN M · 2016 to 2019
$2.2M
European Research Council 340964NIGMS NIH HHS R01 GM120358
6 · The paper itself

Abstract

Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes ranging from metabolic efficiency to lifespan. Here, we present a 3.3-Å-resolution cryo-EM structure of yeast Maf1 bound to Pol III, establishing that Maf1 sequesters Pol III elements involved in transcription initiation and binds the mobile C34 winged helix 2 domain, sealing off the active site. The Maf1 binding site overlaps with that of TFIIIB in the preinitiation complex.

Indexed as

Transcription, GeneticAmino Acid SequenceBinding SitesCloning, MolecularCryoelectron MicroscopyEscherichia coliGene ExpressionGenetic VectorsHumansModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein SubunitsRecombinant ProteinsMAF1 protein, humanMAF1 protein, S cerevisiaeProtein SubunitsRecombinant ProteinsRepressor ProteinsRNA Polymerase IIISaccharomyces cerevisiae ProteinsTranscription FactorsTranscription Factor TFIIIB

Identifiers

PMID32066962
PMCPMC7104376
OpenAlexW3007561110

What OpenQuestion holds

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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.