Evidence map›Paper›PMID 26721860›Full record

ArticleThe Plant cell2016

Reduced Biosynthesis of Digalactosyldiacylglycerol, a Major Chloroplast Membrane Lipid, Leads to Oxylipin Overproduction and Phloem Cap Lignification in Arabidopsis.

Yang-Tsung Lin, Lih-Jen Chen, Cornelia Herrfurth, Ivo Feussner, Hsou-Min Li

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

33 citing papers in PubMed, 71 citations in OpenAlex.

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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

5 authors at 2 institutions in 2 countries.

Yang-Tsung LinInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan.ORCID http://orcid.org/0000-0001-8826-4251
Lih-Jen ChenInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan.
Cornelia HerrfurthGeorg-August-University Goettingen, Albrecht-von-Haller-Institute for Plant Sciences, Department of Plant Biochemistry, D-37077 Goettingen, Germany.
Ivo FeussnerGeorg-August-University Goettingen, Albrecht-von-Haller-Institute for Plant Sciences, Department of Plant Biochemistry, D-37077 Goettingen, Germany Georg-August-University Goettingen, Goettingen Center for Molecular Biosciences, Department of Plant Biochemistry, D-37077 Goettingen, Germany.ORCID http://orcid.org/0000-0002-9888-7003
Hsou-Min LiInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan mbhmli@gate.sinica.edu.tw.ORCID http://orcid.org/0000-0002-0211-7339
Institute of Molecular Biology, Academia Sinica · TWUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DIGALACTOSYLDIACYLGLYCEROL SYNTHASE1 (DGD1) is a chloroplast outer membrane protein responsible for the biosynthesis of the lipid digalactosyldiacylglycerol (DGDG) from monogalactosyldiacylglycerol (MGDG). The Arabidopsis thaliana dgd1 mutants have a greater than 90% reduction in DGDG content, reduced photosynthesis, and altered chloroplast morphology. However, the most pronounced visible phenotype is the extremely short inflorescence stem, but how deficient DGDG biosynthesis causes this phenotype is unclear. We found that, in dgd1 mutants, phloem cap cells were lignified and jasmonic acid (JA)-responsive genes were highly upregulated under normal growth conditions. The coronative insensitive1 dgd1 and allene oxide synthase dgd1 double mutants no longer exhibited the short inflorescence stem and lignification phenotypes but still had the same lipid profile and reduced photosynthesis as dgd1 single mutants. Hormone and lipidomics analyses showed higher levels of JA, JA-isoleucine, 12-oxo-phytodienoic acid, and arabidopsides in dgd1 mutants. Transcript and protein level analyses further suggest that JA biosynthesis in dgd1 is initially activated through the increased expression of genes encoding 13-lipoxygenases (LOXs) and phospholipase A-Iγ3 (At1g51440), a plastid lipase with a high substrate preference for MGDG, and is sustained by further increases in LOX and allene oxide cyclase mRNA and protein levels. Our results demonstrate a link between the biosynthesis of DGDG and JA.

Indexed as

Biosynthetic PathwaysAllelesArabidopsisChloroplastsCyclopentanesEthylenesGalactolipidsGene Expression Regulation, PlantGenes, PlantIndoleacetic AcidsInflorescenceLigninMembrane LipidsMutationOxylipinsPhenotypeCyclopentanesdigalactosyldiacylglycerolethyleneEthylenesGalactolipidsIndoleacetic Acidsjasmonic acidLigninMembrane LipidsOxylipins

Identifiers

PMID26721860
PMCPMC4746690
OpenAlexW2253120304

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.