Evidence map›Paper›PMID 26105654›Full record

ArticlePlanta2015

Biochemical characterization of allene oxide synthases from the liverwort Marchantia polymorpha and green microalgae Klebsormidium flaccidum provides insight into the evolutionary divergence of the plant CYP74 family.

Takao Koeduka, Kimitsune Ishizaki, Cynthia Mugo Mwenda, Koichi Hori, Yuko Sasaki-Sekimoto, Hiroyuki Ohta, Takayuki Kohchi, Kenji Matsui

Abstract read
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In one paragraph

Article in Planta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
16.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

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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

18 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Cytochromes P450 evolution in the plant terrestrialization context.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
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  6. CRISPR/Cas9-mediated disruption ofPlant biotechnology (Tokyo, Japan) · 2022
    Article
  7. Review
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  9. Article
  10. Green Leaf Volatile-Burst inFrontiers in plant science · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Takao KoedukaDepartment of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 753-8515, Japan. takaori@yamaguchi-u.ac.jp.
Kimitsune IshizakiGraduate School of Science, Kobe University, Kobe, 657-8501, Japan.
Cynthia Mugo MwendaApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Koichi HoriCenter for Biological Resources and Informatics, Tokyo Institute of Technology, Kanagawa, 226-8501, Japan.
Yuko Sasaki-SekimotoEarth-Life Science Institute, Tokyo Institute of Technology, Tokyo, 152-8551, Japan.
Hiroyuki OhtaCenter for Biological Resources and Informatics, Tokyo Institute of Technology, Kanagawa, 226-8501, Japan.
Takayuki KohchiGraduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Kenji MatsuiDepartment of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 753-8515, Japan. matsui@yamaguchi-u.ac.jp.
Tokyo Institute of Technology · JPYamaguchi University · JPKobe University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MAIN

conclusionAllene oxide synthases (AOSs) were isolated from liverworts and charophytes. These AOSs exhibited enzymatic properties similar to those of angiosperms but formed a distinct phylogenetic clade. Allene oxide synthase (AOS) and hydroperoxide lyase (HPL) mediate the formation of precursors of jasmonates and carbon-six volatiles, respectively. AOS and HPL utilize fatty acid hydroperoxides and belong to the plant cytochrome P450 74 (CYP74) family that mediates plant defense against herbivores, pathogens, or abiotic stresses. Although members of the CYP74 family have been reported in mosses and other species, the evolution and function of multiple CYP74 genes in plants remain elusive. Here, we show that the liverwort Marchantia polymorpha belongs to a basal group in the evolution of land plants; has two closely related proteins (59% identity), MpAOS1 and MpAOS2, that are similar to moss PpAOS1 (49 and 47% identity, respectively); and exhibits AOS activity but not HPL activity. We also found that the green microalgae Klebsormidium flaccidum, consist of multicellular and non-branching filaments, contains an enzyme, KfAOS, that is similar to PpAOS1 (37% identity), and converts 13-hydroperoxide of linolenic acid to 12-oxo-phytodienoic acid in a coupled reaction with allene oxide cyclase. Phylogenetic analysis showed two evolutionarily distinct clusters. One cluster comprised AOS and HPL from charophytic algae, liverworts, and mosses, including MpAOSs and KfAOS. The other cluster was formed by angiosperm CYP74. Our results suggest that plant CYP74 enzymes with AOS, HPL, and divinyl ether synthase activities have arisen multiple times and in the two different clades, which occurred prior to the divergence of the flowering plant lineage.

Indexed as

Evolution, MolecularCytochrome P-450 Enzyme SystemIntramolecular OxidoreductasesMarchantiaMicroalgaePlant ProteinsCytochrome P-450 Enzyme Systemdivinyl ether synthasehydroperoxide isomeraseIntramolecular OxidoreductasesPlant ProteinsAllene oxide synthaseC8 volatilesCYP74Hydroperoxide lyasePlant evolution

Identifiers

PMID26105654
OpenAlexW2086377488

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.