Evidence map›Paper›PMID 34919733›Full record

ArticlePlant physiology2022

Alternative oxidase (AOX) 1a and 1d limit proline-induced oxidative stress and aid salinity recovery in Arabidopsis.

Glenda Guek Khim Oh, Brendan M O'Leary, Santiago Signorelli, A Harvey Millar

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Review
  3. Genome-wide identification ofFrontiers in plant science · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Genome-Wide Identification and Characterization ofPlants (Basel, Switzerland) · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Please, carefully, pass the P5C.Journal of experimental botany · 2024
    Article
  13. Determination of Free Proline in Plants.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  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

4 authors at 2 institutions in 3 countries.

Glenda Guek Khim OhAustralian Research Council Centre of Excellence in Plant Energy Biology, School of Molecular Sciences, University of Western Australia, Crawley WA 6009, Australia.ORCID 0000-0001-6102-061X
Brendan M O'LearyAustralian Research Council Centre of Excellence in Plant Energy Biology, School of Molecular Sciences, University of Western Australia, Crawley WA 6009, Australia.ORCID 0000-0002-8770-155X
Santiago SignorelliAustralian Research Council Centre of Excellence in Plant Energy Biology, School of Molecular Sciences, University of Western Australia, Crawley WA 6009, Australia.ORCID 0000-0002-1854-3164
A Harvey MillarAustralian Research Council Centre of Excellence in Plant Energy Biology, School of Molecular Sciences, University of Western Australia, Crawley WA 6009, Australia.ORCID 0000-0001-9679-1473
Australian Research Council · AUAgriculture and Agri-Food Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proline (Pro) catabolism and reactive oxygen species production have been linked in mammals and Caenorhabditis elegans, while increases in leaf respiration rate follow Pro exposure in plants. Here, we investigated how alternative oxidases (AOXs) of the mitochondrial electron transport chain accommodate the large, atypical flux resulting from Pro catabolism and limit oxidative stress during Pro breakdown in mature Arabidopsis (Arabidopsis thaliana) leaves. Following Pro treatment, AOX1a and AOX1d accumulate at transcript and protein levels, with AOX1d approaching the level of the typically dominant AOX1a isoform. We therefore sought to determine the function of both AOX isoforms under Pro respiring conditions. Oxygen consumption rate measurements in aox1a and aox1d leaves suggested these AOXs can functionally compensate for each other to establish enhanced AOX catalytic capacity in response to Pro. Generation of aox1a.aox1d lines showed complete loss of AOX proteins and activity upon Pro treatment, yet full respiratory induction in response to Pro remained possible via the cytochrome pathway. However, aox1a.aox1d leaves displayed symptoms of elevated oxidative stress and suffered increased oxidative damage during Pro metabolism compared to the wild-type (WT) or the single mutants. During recovery from salt stress, when relatively high rates of Pro catabolism occur naturally, photosynthetic rates in aox1a.aox1d recovered slower than in the WT or the single aox lines, showing that both AOX1a and AOX1d are beneficial for cellular metabolism during Pro drawdown following osmotic stress. This work provides physiological evidence of a beneficial role for AOX1a but also the less studied AOX1d isoform in allowing safe catabolism of alternative respiratory substrates like Pro.

Indexed as

Adaptation, PhysiologicalArabidopsisElectron Transport Chain Complex ProteinsGene Expression Regulation, PlantGenes, PlantGenotypeMitochondriaMutationOxidative StressOxidoreductasesPharmacogenomic VariantsProlineReactive Oxygen SpeciesSalt StressElectron Transport Chain Complex ProteinsOxidoreductasesProlineReactive Oxygen Species

Identifiers

PMID34919733
PMCPMC8896607
OpenAlexW4200288072

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.