Evidence map›Paper›PMID 21784950›Full record

ArticleThe Plant cell2011

Perturbation of Arabidopsis amino acid metabolism causes incompatibility with the adapted biotrophic pathogen Hyaloperonospora arabidopsidis.

Johannes Stuttmann, Hans-Michael Hubberten, Steffen Rietz, Jagreet Kaur, Paul Muskett, Raphael Guerois, Pawel Bednarek, Rainer Hoefgen, Jane E Parker

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
17.2field-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

54 citing papers in PubMed, 118 citations in OpenAlex.

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  10. New Insight into Aspartate Metabolic Pathways inInternational journal of molecular sciences · 2022
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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

9 authors at 3 institutions in 2 countries.

Johannes StuttmannDepartment of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, D-50829 Cologne, Germany.
Hans-Michael Hubberten
Steffen Rietz
Jagreet Kaur
Paul Muskett
Raphael Guerois
Pawel Bednarek
Rainer Hoefgen
Jane E Parker
Max Planck Institute for Plant Breeding Research · DEMax Planck Society · DECommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reliance of biotrophic pathogens on living plant tissues to propagate implies strong interdependence between host metabolism and nutrient uptake by the pathogen. However, factors determining host suitability and establishment of infection are largely unknown. We describe a loss-of-inhibition allele of ASPARTATE KINASE2 and a loss-of-function allele of DIHYDRODIPICOLINATE SYNTHASE2 identified in a screen for Arabidopsis thaliana mutants with increased resistance to the obligate biotrophic oomycete Hyaloperonospora arabidopsidis (Hpa). Through different molecular mechanisms, these mutations perturb amino acid homeostasis leading to overaccumulation of the Asp-derived amino acids Met, Thr, and Ile. Although detrimental for the plant, the mutations do not cause defense activation, and both mutants retain full susceptibility to the adapted obligate biotrophic fungus Golovinomyces orontii (Go). Chemical treatments mimicking the mutants' metabolic state identified Thr as the amino acid suppressing Hpa but not Go colonization. We conclude that perturbations in amino acid homeostasis render the mutant plants unsuitable as an infection substrate for Hpa. This may be explained by deployment of the same amino acid biosynthetic pathways by oomycetes and plants. Our data show that the plant host metabolic state can, in specific ways, influence the ability of adapted biotrophic strains to cause disease.

Indexed as

Amino AcidsAmino Acid SequenceArabidopsisArabidopsis ProteinsAspartate KinaseCarrier ProteinsDisease ResistanceHomeostasisHost-Pathogen InteractionsHydro-LyasesIntracellular Signaling Peptides and ProteinsModels, MolecularMolecular Sequence DataMutationOomycetesPlant Diseases4-hydroxy-tetrahydrodipicolinate synthaseAmino AcidsArabidopsis ProteinsAspartate KinaseCarrier ProteinsHydro-LyasesIntracellular Signaling Peptides and ProteinsPBS2 protein, Arabidopsis

Identifiers

PMID21784950
PMCPMC3226217
OpenAlexW2136443154

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.