Evidence map›Paper›PMID 30690555›Full record

ArticleJournal of experimental botany2019

Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana.

Stephan Pollmann, Armin Springer, Sachin Rustgi, Diter von Wettstein, ChulHee Kang, Christiane Reinbothe, Steffen Reinbothe

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.2field-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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Maize LipoxygenasePlants (Basel, Switzerland) · 2026
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  5. Protein assemblies in theFrontiers in plant science · 2024
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  7. Review
  8. Article
  9. Article
  10. Article
  11. Production of the Green Leaf Volatile (Plants (Basel, Switzerland) · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Biochemical Characterization of 13-Lipoxygenases ofInternational journal of molecular sciences · 2021
    Article
  17. Article
  18. Article
  19. Review
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

7 authors at 4 institutions in 4 countries.

Stephan PollmannCentro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid (UPM) - Instituto Nacional de Investigación y Tecnología Agraria y Alimentación (INIA), Campus de Montegancedo, Pozuelo de Alarcón (Madrid), Spain.
Armin SpringerMedizinische Biologie und Elektronenmikroskopisches Zentrum (EMZ), Universitätsmedizin Rostock, Rostock, Germany.
Sachin RustgiDepartment of Plant and Environmental Sciences, Pee Dee Research and Education Center, Clemson University, Florence, SC, USA.
Diter von WettsteinDepartment of Crop and Soil Sciences, Washington State University, Pullman, WA, USA.
ChulHee KangDepartment of Chemistry, Washington State University, Pullman, WA, USA.
Christiane ReinbotheLaboratoire de Génétique Moléculaire des Plantes, Université Grenoble Alpes, CEDEX, France.
Steffen ReinbotheLaboratoire de Génétique Moléculaire des Plantes, Université Grenoble Alpes, CEDEX, France.
Washington State University · USUniversité Grenoble Alpes · FRInstituto Nacional de Investigación y Tecnología Agraria y Alimentaria · ESUniversitätsmedizin Rostock · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxygenated membrane fatty acid derivatives termed oxylipins play important roles in plant defense against biotic and abiotic cues. Plants challenged by insect pests, for example, synthesize a blend of different defense compounds that include volatile aldehydes and jasmonic acid (JA), among others. Because all oxylipins are derived from the same pathway, we investigated how their synthesis might be regulated, focusing on two closely related atypical cytochrome P450 enzymes designated CYP74A and CYP74B, respectively, allene oxide synthase (AOS) and hydroperoxide lyase (HPL). These enzymes compete for the same substrate but give rise to different products: the final product of the AOS branch of the oxylipin pathway is JA, while those of the HPL branch comprise volatile aldehydes and alcohols. AOS and HPL are plastid envelope enzymes in Arabidopsis thaliana but accumulate at different locations. Biochemical experiments identified AOS as a constituent of complexes also containing lipoxygenase 2 (LOX2) and allene oxide cyclase (AOC), which catalyze consecutive steps in JA precursor biosynthesis, while excluding the concurrent HPL reaction. Based on published X-ray data, the structure of this complex was modelled and amino acids involved in catalysis and subunit interactions predicted. Genetic studies identified the microRNA 319-regulated clade of TCP (TEOSINTE BRANCHED/CYCLOIDEA/PCF) transcription factor genes and CORONATINE INSENSITIVE 1 (COI1) as controlling JA production through the LOX2-AOS-AOC2 complex. Together, our results define a molecular branch point in oxylipin biosynthesis that allows fine-tuning of the plant's defense machinery in response to biotic and abiotic stimuli.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplast ProteinsCytochrome P-450 Enzyme SystemMixed Function OxygenasesOxylipinsPlastidsArabidopsis ProteinsAt5g42650 protein, ArabidopsisChloroplast ProteinsCytochrome P-450 Enzyme SystemHPL1 protein, ArabidopsisMixed Function OxygenasesOxylipinsallene oxide cyclaseAllene oxide synthasechloroplast envelope protein complexhydroperoxide lyaselipoxygenasemetabolite channelingplant defense

Identifiers

PMID30690555
PMCPMC6411374
OpenAlexW2951465121

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.