Evidence map›Paper›PMID 21504904›Full record

ArticleThe Journal of biological chemistry2011

The pentatricopeptide repeat protein OTP87 is essential for RNA editing of nad7 and atp1 transcripts in Arabidopsis mitochondria.

Kamel Hammani, Catherine Colas des Francs-Small, Mizuki Takenaka, Sandra K Tanz, Kenji Okuda, Toshiharu Shikanai, Axel Brennicke, Ian Small

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.1field-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

38 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
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  3. Review
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  6. Review
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  8. GRP23 plays a core role in E-type editosomes via interacting with MORFs and atypical PPR-DYWs inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Targeted base editing in the mitochondrial genome ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The Analysis of the Editing Defects in thePlants (Basel, Switzerland) · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. 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 4 institutions in 4 countries.

Kamel HammaniAustralian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009 Western Australia, Australia. khammani@uoregon.edu
Catherine Colas des Francs-Small
Mizuki Takenaka
Sandra K Tanz
Kenji Okuda
Toshiharu Shikanai
Axel Brennicke
Ian Small
ARC Centre of Excellence in Plant Energy Biology · AUAustralian Research Council · AUKyoto University · JPUniversität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plant organelles, RNA editing is a post-transcriptional mechanism that converts specific cytidines to uridines in RNA of both mitochondria and plastids, altering the information encoded by the gene. The cytidine to be edited is determined by a cis-element surrounding the editing site that is specifically recognized and bound by a trans-acting factor. All the trans-acting editing factors identified so far in plant organelles are members of a large protein family, the pentatricopeptide repeat (PPR) proteins. We have identified the Organelle Transcript Processing 87 (OTP87) gene, which is required for RNA editing of the nad7-C24 and atp1-C1178 sites in Arabidopsis mitochondria. OTP87 encodes an E-subclass PPR protein with an unusually short E-domain. The recombinant protein expressed in Escherichia coli specifically binds to RNAs comprising 30 nucleotides upstream and 10 nucleotides downstream of the nad7-C24 and atp1-C1178 editing sites. The loss-of-function of OTP87 results in small plants with growth and developmental delays. In the otp87 mutant, the amount of assembled respiratory complex V (ATP synthase) is highly reduced compared with the wild type suggesting that the amino acid alteration in ATP1 caused by loss of editing at the atp1-C1178 site affects complex V assembly in mitochondria.

Indexed as

RNA EditingArabidopsisArabidopsis ProteinsBinding SitesChlorophyllEscherichia coliGene Expression Regulation, PlantGenetic Complementation TestMitochondriaMitochondrial Proton-Translocating ATPasesModels, GeneticMutationNADH DehydrogenasePeptidesPhenotypePlant ProteinsArabidopsis ProteinsATP1 protein, ArabidopsisChlorophyllMitochondrial Proton-Translocating ATPasesNAD7 protein, ArabidopsisNADH DehydrogenaseOTP87 protein, ArabidopsisPeptidesPlant ProteinsProton-Translocating ATPasesRNA-Binding Proteins

Identifiers

PMID21504904
PMCPMC3122196
OpenAlexW2091434928

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.