Evidence map›Paper›PMID 33029918›Full record

ArticleMolecular plant pathology2020

AtPME17 is a functional Arabidopsis thaliana pectin methylesterase regulated by its PRO region that triggers PME activity in the resistance to Botrytis cinerea.

Daniele Del Corpo, Maria R Fullone, Rossella Miele, Mickaël Lafond, Daniela Pontiggia, Sacha Grisel, Sylvie Kieffer-Jaquinod, Thierry Giardina, Daniela Bellincampi, Vincenzo Lionetti

Open access · goldAbstract read
In one paragraph

Article in Molecular plant pathology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
12.7field-weighted citation impact, top 1% 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

48 citing papers in PubMed, 90 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

10 authors at 5 institutions in 2 countries.

Daniele Del CorpoDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, Rome, Italy.
Maria R FulloneDepartment of Biochemical Sciences "A. Rossi Fanelli", Pasteur Institute-Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome, Italy.
Rossella MieleDepartment of Biochemical Sciences "A. Rossi Fanelli", Pasteur Institute-Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome, Italy.
Mickaël LafondAix-Marseille University, CNRS, Marseille, France.
Daniela PontiggiaDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, Rome, Italy.
Sacha GriselBiodiversité et Biotechnologie Fongiques, INRA, Aix Marseille University, UMR1163, Marseille, France.
Sylvie Kieffer-JaquinodUniversity Grenoble Alpes, CEA, INSERM, Grenoble, France.
Thierry GiardinaAix-Marseille University, CNRS, Marseille, France.
Daniela BellincampiDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, Rome, Italy.
Vincenzo LionettiDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, Rome, Italy.ORCID 0000-0002-2262-1479
Sapienza University of Rome · ITCentre National de la Recherche Scientifique · FRIstituto Pasteur · ITAix-Marseille Université · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pectin is synthesized in a highly methylesterified form in the Golgi cisternae and partially de-methylesterified in muro by pectin methylesterases (PMEs). Arabidopsis thaliana produces a local and strong induction of PME activity during the infection of the necrotrophic fungus Botrytis cinerea. AtPME17 is a putative A. thaliana PME highly induced in response to B. cinerea. Here, a fine tuning of AtPME17 expression by different defence hormones was identified. Our genetic evidence demonstrates that AtPME17 strongly contributes to the pathogen-induced PME activity and resistance against B. cinerea by triggering jasmonic acid-ethylene-dependent PDF1.2 expression. AtPME17 belongs to group 2 isoforms of PMEs characterized by a PME domain preceded by an N-terminal PRO region. However, the biochemical evidence for AtPME17 as a functional PME is still lacking and the role played by its PRO region is not known. Using the Pichia pastoris expression system, we demonstrate that AtPME17 is a functional PME with activity favoured by an increase in pH. AtPME17 performs a blockwise pattern of pectin de-methylesterification that favours the formation of egg-box structures between homogalacturonans. Recombinant AtPME17 expression in Escherichia coli reveals that the PRO region acts as an intramolecular inhibitor of AtPME17 activity.

Indexed as

ArabidopsisArabidopsis ProteinsBotrytisCarboxylic Ester HydrolasesCyclopentanesDefensinsEscherichia coliEthylenesGene ExpressionIsoenzymesOxylipinsPectinsPlant DiseasesPromoter Regions, GeneticRecombinant ProteinsSaccharomycetalesArabidopsis ProteinsAt5g44420 protein, ArabidopsisCarboxylic Ester HydrolasesCyclopentanesDefensinsethyleneEthylenesIsoenzymesjasmonic acidOxylipinsPectinsPME17 protein, Arabidopsispolygalacturonic acidRecombinant ProteinsArabidopsis thalianaBotrytis cinereacell wall integritypectin methylesterasesplant immunity

Identifiers

PMID33029918
PMCPMC7694680
OpenAlexW3092639320

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.