Evidence map›Paper›PMID 34712911›Full record

ArticleNature catalysis2021

DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis.

Mizuki Takenaka, Sachi Takenaka, Tatjana Barthel, Brody Frink, Sascha Haag, Daniil Verbitskiy, Bastian Oldenkott, Mareike Schallenberg-Rüdinger, Christian G Feiler, Manfred S Weiss and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Nature catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  5. Structures of pentatricopeptide repeat proteins.Acta crystallographica. Section F, Structural biology communications · 2026
    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

12 authors at 5 institutions in 2 countries.

Mizuki TakenakaDepartment of Botany, Graduate School of Science, Kyoto University, Kyoto, Japan.ORCID https://orcid.org/0000-0002-3242-5092
Sachi TakenakaDepartment of Botany, Graduate School of Science, Kyoto University, Kyoto, Japan.ORCID https://orcid.org/0000-0001-9808-385X
Tatjana BarthelUniversity of Greifswald, Molecular Structural Biology, Greifswald, Germany.
Brody FrinkDepartment of Botany, Graduate School of Science, Kyoto University, Kyoto, Japan.ORCID https://orcid.org/0000-0001-7422-4347
Sascha HaagMolekulare Botanik, Universität Ulm, Ulm, Germany.
Daniil VerbitskiyMolekulare Botanik, Universität Ulm, Ulm, Germany.
Bastian OldenkottInstitut für Zelluläre und Molekulare Botanik, Abteilung Molekulare Evolution, University of Bonn, Bonn, Germany.
Mareike Schallenberg-RüdingerInstitut für Zelluläre und Molekulare Botanik, Abteilung Molekulare Evolution, University of Bonn, Bonn, Germany.ORCID https://orcid.org/0000-0002-6874-4722
Christian G FeilerHelmholtz-Zentrum Berlin für Materialien und Energie, Macromolecular Crystallography, Berlin, Germany.
Manfred S WeissHelmholtz-Zentrum Berlin für Materialien und Energie, Macromolecular Crystallography, Berlin, Germany.ORCID https://orcid.org/0000-0002-2362-7047
Gottfried J PalmUniversity of Greifswald, Molecular Structural Biology, Greifswald, Germany.ORCID https://orcid.org/0000-0003-0329-0413
Gert WeberHelmholtz-Zentrum Berlin für Materialien und Energie, Macromolecular Crystallography, Berlin, Germany.ORCID https://orcid.org/0000-0003-3624-1060
Helmholtz-Zentrum Berlin für Materialien und Energie · DEKyoto University · JPUniversität Ulm · DEUniversity of Bonn · DEUniversität Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA editosomes selectively deaminate cytidines to uridines in plant organellar transcripts-mostly to restore protein functionality and consequently facilitate mitochondrial and chloroplast function. The RNA editosomal pentatricopeptide repeat proteins serve target RNA recognition, whereas the intensively studied DYW domain elicits catalysis. Here we present structures and functional data of a DYW domain in an inactive ground state and activated. DYW domains harbour a cytidine deaminase fold and a C-terminal DYW motif, with catalytic and structural zinc atoms, respectively. A conserved gating domain within the deaminase fold regulates the active site sterically and mechanistically in a process that we termed gated zinc shutter. Based on the structures, an autoinhibited ground state and its activation are cross-validated by RNA editing assays and differential scanning fluorimetry. We anticipate that, in vivo, the framework of an active plant RNA editosome triggers the release of DYW autoinhibition to ensure a controlled and coordinated cytidine deamination playing a key role in mitochondrial and chloroplast homeostasis.

Identifiers

PMID34712911
PMCPMC7611903
OpenAlexW3173195765

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LicenceCC BY
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Registered trials

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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.