Evidence map›Paper›PMID 25056921›Full record

ArticlePlant physiology2014

The reductase activity of the Arabidopsis caleosin RESPONSIVE TO DESSICATION20 mediates gibberellin-dependent flowering time, abscisic acid sensitivity, and tolerance to oxidative stress.

Elizabeth Blée, Benoît Boachon, Michel Burcklen, Marina Le Guédard, Abdulsamie Hanano, Dimitri Heintz, Jürgen Ehlting, Cornelia Herrfurth, Ivo Feussner, Jean-Jacques Bessoule

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.3field-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

39 citing papers in PubMed, 68 citations in OpenAlex.

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  17. Plants (Basel, Switzerland) · 2021
    Article
  18. Evolution and Stress Responses ofFrontiers in plant science · 2021
    Article
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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

10 authors at 4 institutions in 2 countries.

Elizabeth BléeInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.) elizabeth.blee@ibmp-cnrs.unistra.fr.
Benoît BoachonInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Michel BurcklenInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Marina Le GuédardInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Abdulsamie HananoInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Dimitri HeintzInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Jürgen EhltingInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Cornelia HerrfurthInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Ivo FeussnerInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Jean-Jacques BessouleInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche 2357-Université de Strasbourg, 67083 Strasbourg cedex, France (E.B., B.B., M.B., A.H., D.H., J.E.)Laboratoire de Biogénèse Membranaire, Bâtiment A3-Institut National de la Recherche Agronomique Bordeaux Aquitaine, 33140 Villenave d'Ornon, France (M.L.G., J.-J.B.); andGeorg-August-University, Albrecht-von-Haller Institute, Department of Plant Biochemistry, 37077 Goettingen, Germany (C.H., I.F.).
Institut de Biologie Moléculaire des Plantes · FRInstitut National de la Recherche Agronomique · MALaboratoire de Biogenèse Membranaire · FRUniversité de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Contrasting with the wealth of information available on the multiple roles of jasmonates in plant development and defense, knowledge about the functions and the biosynthesis of hydroxylated oxylipins remains scarce. By expressing the caleosin RESPONSIVE TO DESSICATION20 (RD20) in Saccharomyces cerevisiae, we show that the recombinant protein possesses an unusual peroxygenase activity with restricted specificity toward hydroperoxides of unsaturated fatty acid. Accordingly, Arabidopsis (Arabidopsis thaliana) plants overexpressing RD20 accumulate the product 13-hydroxy-9,11,15-octadecatrienoic acid, a linolenate-derived hydroxide. These plants exhibit elevated levels of reactive oxygen species (ROS) associated with early gibberellin-dependent flowering and abscisic acid hypersensitivity at seed germination. These phenotypes are dependent on the presence of active RD20, since they are abolished in the rd20 null mutant and in lines overexpressing RD20, in which peroxygenase was inactivated by a point mutation of a catalytic histidine residue. RD20 also confers tolerance against stress induced by Paraquat, Rose Bengal, heavy metal, and the synthetic auxins 1-naphthaleneacetic acid and 2,4-dichlorophenoxyacetic acid. Under oxidative stress, 13-hydroxy-9,11,15-octadecatrienoic acid still accumulates in RD20-overexpressing lines, but this lipid oxidation is associated with reduced ROS levels, minor cell death, and delayed floral transition. A model is discussed where the interplay between fatty acid hydroxides generated by RD20 and ROS is counteracted by ethylene during development in unstressed environments.

Indexed as

Plant DevelopmentAbscisic AcidArabidopsisArabidopsis ProteinsCalcium-Binding ProteinsEthylenesFatty Acids, UnsaturatedFlowersGerminationGibberellinsOxidative StressPlant DormancyReactive Oxygen SpeciesSubstrate Specificity13-Hydroxy-octadecatrienoic acidAbscisic AcidArabidopsis ProteinsCalcium-Binding ProteinsethyleneEthylenesFatty Acids, UnsaturatedGibberellinsRD20 protein, ArabidopsisReactive Oxygen Species

Identifiers

PMID25056921
PMCPMC4149700
OpenAlexW1975165107

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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.