Evidence map›Paper›PMID 20729481›Full record

ArticleJournal of experimental botany2010

Molecular cloning and characterization of a novel tomato xylosyltransferase specific for gentisic acid.

Susana Tárraga, Purificación Lisón, María Pilar López-Gresa, Cristina Torres, Ismael Rodrigo, José María Bellés, Vicente Conejero

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 16% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

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  7. Plant physiology · 2017
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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

7 authors at 1 institution in 1 country.

Susana TárragaInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia, Consejo Superior de Investigaciones Científicas, Ciudad Politécnica de la Innovación, Ed 8E, E-46022 Valencia, Spain.
Purificación Lisón
María Pilar López-Gresa
Cristina Torres
Ismael Rodrigo
José María Bellés
Vicente Conejero
Universitat Politècnica de València · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The importance of salicylic acid (SA) in the signal transduction pathway of plant disease resistance has been well documented in many incompatible plant-pathogen interactions, but less is known about signalling in compatible interactions. In this type of interaction, tomato plants have been found to accumulate high levels of 2,5-dihydroxybenzoic acid (gentisic acid, GA), a metabolic derivative of SA. Exogenous GA treatments induce in tomato plants a set of PR proteins that differ from those induced by salicylic acid. While SA accumulates in tomato plants mainly as 2-O-β-D-glucoside, GA has only been found as 5-O-β-D-xyloside. To characterize this step of the GA signalling pathway further, the present work focuses on the study of the GA-conjugating activity in tomato plants. A gentisate glycosyltransferase (GAGT) cDNA has been isolated and overexpressed in Pichia pastoris, and GA-conjugating activity was confirmed by detecting the xylosylated GA. The purified plant protein is highly specific for GA, showing no activity toward many other phenolic compounds, including SA. In addition, it shows an outstanding selectivity for UDP-xylose as the sugar donor, which differentiates this enzyme from most glycosyltransferases. Both the GA-conjugating activity and the corresponding mRNA show a strong, rapid, and transient induction upon treatment of tomato plants with GA or SA. Furthermore, its expression is rapidly induced by compatible infections. However, neither the gene nor the activity seems to respond to incompatible infections or wounding. The unique properties of this new glycosyltransferase suggest a specific role in regulating the free GA levels in compatible plant-pathogen interactions.

Indexed as

AcetatesCloning, MolecularCyclopentanesDNA, ComplementaryEnzyme InductionGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGentisatesOxylipinsPentosyltransferasesPseudomonas syringaeRecombinant ProteinsRNA, MessengerSalicylic AcidSolanum lycopersicumStructural Homology, Protein2,5-dihydroxybenzoic acidAcetatesCyclopentanesDNA, ComplementaryGentisatesmethyl jasmonateOxylipinsPentosyltransferasesRecombinant ProteinsRNA, MessengerSalicylic AcidUDP Xylose-Protein Xylosyltransferase

Identifiers

PMID20729481
PMCPMC2955746
OpenAlexW2146687030

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.