Evidence map›Paper›PMID 34037778›Full record

ArticleNucleic acids research2021

In vivo stabilization of endogenous chloroplast RNAs by customized artificial pentatricopeptide repeat proteins.

Nikolay Manavski, Sébastien Mathieu, Margarita Rojas, Louis-Valentin Méteignier, Andreas Brachmann, Alice Barkan, Kamel Hammani

Abstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. The plant cytosolic mPlant communications · 2023
    Article
  11. Review
  12. Article
  13. Plant organellar RNA maturation.The Plant cell · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
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.

Nikolay ManavskiInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.
Sébastien MathieuInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.
Margarita RojasInstitute of Molecular Biology, University of Oregon, Eugene, OR 97403 USA.
Louis-Valentin MéteignierInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.
Andreas BrachmannGenetics, Faculty of Biology, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried Germany.
Alice BarkanInstitute of Molecular Biology, University of Oregon, Eugene, OR 97403 USA.
Kamel HammaniInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.ORCID 0000-0001-5759-5955

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pentatricopeptide repeat (PPR) proteins are helical repeat-proteins that bind RNA in a modular fashion with a sequence-specificity that can be manipulated by the use of an amino acid code. As such, PPR repeats are promising scaffolds for the design of RNA binding proteins for synthetic biology applications. However, the in vivo functional capabilities of artificial PPR proteins built from consensus PPR motifs are just starting to be explored. Here, we report in vivo functions of an artificial PPR protein, dPPRrbcL, made of consensus PPR motifs that were designed to bind a sequence near the 5' end of rbcL transcripts in Arabidopsis chloroplasts. We used a functional complementation assay to demonstrate that this protein bound its intended RNA target with specificity in vivo and that it substituted for a natural PPR protein by stabilizing processed rbcL mRNA. We targeted a second protein of analogous design to the petL 5' UTR, where it substituted for the native stabilizing PPR protein PGR3, albeit inefficiently. These results showed that artificial PPR proteins can be engineered to functionally mimic the class of native PPR proteins that serve as physical barriers against exoribonucleases.

Indexed as

5' Untranslated RegionsArabidopsisArabidopsis ProteinsChloroplastsGene ExpressionPlants, Genetically ModifiedProtein BindingProtein EngineeringRecombinant ProteinsRibulose-Bisphosphate CarboxylaseRNA-Binding MotifsRNA-Binding ProteinsRNA, Chloroplast5' Untranslated RegionsArabidopsis ProteinsPDM2 protein, ArabidopsisPGR3 protein, ArabidopsisRbcL protein, plastidRecombinant ProteinsRibulose-Bisphosphate CarboxylaseRNA-Binding ProteinsRNA, Chloroplast

Identifiers

PMID34037778
PMCPMC8191804

What Socratic holds

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LicenceCC BY-NC
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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 Socratic graph.