Evidence map›Paper›PMID 21788362›Full record

ArticlePlant physiology2011

Analysis of a range of catabolic mutants provides evidence that phytanoyl-coenzyme A does not act as a substrate of the electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase complex in Arabidopsis during dark-induced senescence.

Wagner L Araújo, Kimitsune Ishizaki, Adriano Nunes-Nesi, Takayuki Tohge, Tony R Larson, Ina Krahnert, Ilse Balbo, Sandra Witt, Peter Dörmann, Ian A Graham and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. A systematicFrontiers in plant science · 2023
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. PheophorbidePlant physiology · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. The use of metabolomics to dissect plant responses to abiotic stresses.Cellular and molecular life sciences : CMLS · 2012
    Review
  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

12 authors at 4 institutions in 4 countries.

Wagner L AraújoMax Planck Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany.
Kimitsune Ishizaki
Adriano Nunes-Nesi
Takayuki Tohge
Tony R Larson
Ina Krahnert
Ilse Balbo
Sandra Witt
Peter Dörmann
Ian A Graham
Christopher J Leaver
Alisdair R Fernie
University of Bonn · DEKyoto University · JPUniversity of Oxford · GBUniversidade Federal de Viçosa · BR

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

The process of dark-induced senescence in plants is not fully understood, however, the functional involvement of an electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF/ETFQO), has been demonstrated. Recent studies have revealed that the enzymes isovaleryl-coenzyme A (CoA) dehydrogenase and 2-hydroxyglutarate dehydrogenase act as important electron donors to this complex. In addition both enzymes play a role in the breakdown of cellular carbon storage reserves with isovaleryl-CoA dehydrogenase being involved in degradation of the branched-chain amino acids, phytol, and lysine while 2-hydroxyglutarate dehydrogenase is exclusively involved in lysine degradation. Given that the chlorophyll breakdown intermediate phytanoyl-CoA accumulates dramatically both in knockout mutants of the ETF/ETFQO complex and of isovaleryl-CoA dehydrogenase following growth in extended dark periods we have investigated the direct importance of chlorophyll breakdown for the supply of carbon and electrons during this process. For this purpose we isolated three independent Arabidopsis (Arabidopsis thaliana) knockout mutants of phytanoyl-CoA 2-hydroxylase and grew them under the same extended darkness regime as previously used. Despite the fact that these mutants accumulated phytanoyl-CoA and also 2-hydroxyglutarate they exhibited no morphological changes in comparison to the other mutants previously characterized. These results are consistent with a single entry point of phytol breakdown into the ETF/ETFQO system and furthermore suggest that phytol is not primarily metabolized by this pathway. Furthermore analysis of isovaleryl-CoA dehydrogenase/2-hydroxyglutarate dehydrogenase double mutants generated here suggest that these two enzymes essentially account for the entire electron input via the ETF complex.

Indexed as

DarknessMutationAmino AcidsArabidopsisCoenzyme AElectron-Transferring FlavoproteinsOxidoreductasesPhytanic AcidUbiquitinAmino AcidsCoenzyme AElectron-Transferring FlavoproteinsOxidoreductasesPhytanic Acidphytanoyl-coenzyme AUbiquitin

Identifiers

PMID21788362
PMCPMC3221279
OpenAlexW2060208884

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.