Evidence map›Paper›PMID 25583991›Full record

ArticleThe Journal of biological chemistry2015

Selective homo- and heteromer interactions between the multiple organellar RNA editing factor (MORF) proteins in Arabidopsis thaliana.

Anja Zehrmann, Barbara Härtel, Franziska Glass, Eszter Bayer-Császár, Toshihiro Obata, Etienne Meyer, Axel Brennicke, Mizuki Takenaka

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. The ATP Synthase γ Subunit ATPC1 Regulates RNA Editing in Chloroplasts.International journal of molecular sciences · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. MORF9 Functions in Plastid RNA Editing with Tissue Specificity.International journal of molecular sciences · 2019
    Article
  20. Article
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

8 authors at 2 institutions in 1 country.

Anja ZehrmannFrom the Molekulare Botanik, Universität Ulm, 89069 Ulm and.
Barbara HärtelFrom the Molekulare Botanik, Universität Ulm, 89069 Ulm and.
Franziska GlassFrom the Molekulare Botanik, Universität Ulm, 89069 Ulm and.
Eszter Bayer-CsászárFrom the Molekulare Botanik, Universität Ulm, 89069 Ulm and.
Toshihiro Obatathe Max-Planck-Institut für Pflanzenphysiologie, 14476 Potsdam-Golm, Germany.
Etienne Meyerthe Max-Planck-Institut für Pflanzenphysiologie, 14476 Potsdam-Golm, Germany.
Axel BrennickeFrom the Molekulare Botanik, Universität Ulm, 89069 Ulm and.
Mizuki TakenakaFrom the Molekulare Botanik, Universität Ulm, 89069 Ulm and mizuki.takenaka@uni-ulm.de.
Universität Ulm · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA editing in plastids and mitochondria of flowering plants requires pentatricopeptide repeat proteins (PPR proteins) for site recognition and proteins of the multiple organellar RNA editing factor (MORF) family as cofactors. Two MORF proteins, MORF5 and MORF8, are dual-targeted to plastids and mitochondria; two are targeted to plastids, and five are targeted to mitochondria. Pulldown assays from Arabidopsis thaliana tissue culture extracts with the mitochondrial MORF1 and the plastid MORF2 proteins, respectively, both identify the dual-targeted MORF8 protein, showing that these complexes can assemble in the organelles. We have now determined the scope of potential interactions between the various MORF proteins by yeast two-hybrid, in vitro pulldown, and bimolecular fluorescence complementation assays. The resulting MORF-MORF interactome identifies specific heteromeric MORF protein interactions in plastids and in mitochondria. Heteromers are observed for MORF protein combinations affecting a common site, suggesting their functional relevance. Most MORF proteins also undergo homomeric interactions. Submolecular analysis of the MORF1 protein reveals that the MORF-MORF protein connections require the C-terminal region of the central conserved MORF box. This domain has no similarity to known protein modules and may form a novel surface for protein-protein interactions.

Indexed as

Protein Interaction MapsProtein Structure, TertiaryArabidopsisArabidopsis ProteinsMitochondriaPlastidsProtein BindingProtein MultimerizationRNA EditingArabidopsis ProteinsMORF8 protein, ArabidopsisArabidopsis thalianaChloroplastMitochondriaMORF ProteinsProtein-Protein InteractionRNA Editing

Identifiers

PMID25583991
PMCPMC4358279
OpenAlexW2062787447

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.