Evidence map›Paper›PMID 28201607›Full record

ArticleNucleic acids research2017

Crystal structures of the Arabidopsis thaliana organellar RNA editing factors MORF1 and MORF9.

Sascha Haag, Magdalena Schindler, Leona Berndt, Axel Brennicke, Mizuki Takenaka, Gert Weber

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Sascha HaagMolekulare Botanik, Universität Ulm, 89069 Ulm, Germany.
Magdalena SchindlerInstitut für Chemie und Biochemie, Strukturbiochemie, Freie Universität Berlin, Takustrasse 6, 14195 Berlin, Germany.
Leona BerndtUniversität Greifswald, Institut für Biochemie, Molekulare Strukturbiologie, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany.
Axel BrennickeMolekulare Botanik, Universität Ulm, 89069 Ulm, Germany.
Mizuki TakenakaMolekulare Botanik, Universität Ulm, 89069 Ulm, Germany.
Gert WeberInstitut für Chemie und Biochemie, Strukturbiochemie, Freie Universität Berlin, Takustrasse 6, 14195 Berlin, Germany.
Universität Ulm · DEFreie Universität Berlin · DEUniversität Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In flowering plant plastids and mitochondria, multiple organellar RNA editing factor (MORF/RIP) proteins are required at most sites for efficient C to U RNA editing catalyzed by the RNA editosome. MORF proteins harbor a conserved stretch of residues (MORF-box), form homo- and heteromers and interact with selected PPR (pentatricopeptide repeat) proteins, which recognize each editing site. The molecular function of the MORF-box remains elusive since it shares no sequence similarity with known domains. We determined structures of the A. thaliana mitochondrial MORF1 and chloroplast MORF9 MORF-boxes which both adopt a novel globular fold (MORF domain). Our structures state a paradigmatic model for MORF domains and their specific dimerization via a hydrophobic interface. We cross-validate the interface by yeast two-hybrid studies and pulldown assays employing structure-based mutants. We find a structural similarity of the MORF domain to an N-terminal ferredoxin-like domain (NFLD), which confers RNA substrate positioning in bacterial 4-thio-uracil tRNA synthetases, implying direct RNA contacts of MORF proteins during RNA editing. With the MORF1 and MORF9 structures we elucidate a yet unknown fold, corroborate MORF interaction studies, validate the mechanism of MORF multimerization by structure-based mutants and pave the way towards a complete structural characterization of the plant RNA editosome.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsCrystallography, X-RayMitochondriaMolecular Sequence DataProtein DomainsProtein FoldingProtein Structure, TertiaryRNA-Binding ProteinsRNA EditingRNA Recognition Motif ProteinsArabidopsis ProteinsMORF1 protein, ArabidopsisMORF9 protein, ArabidopsisRNA-Binding ProteinsRNA Recognition Motif Proteins

Identifiers

PMID28201607
PMCPMC5416752
OpenAlexW2588227162

What OpenQuestion holds

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LicenceCC BY-NC
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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.