Evidence map›Paper›PMID 42302289›Full record

ArticlePlant physiology2026

Functional divergence and symbiotic significance of nitrate reductase isoforms in Medicago truncatula.

Marc Bosseno, Alexandre Demba, Natasha Horta Araújo, Dominique Colinet, Abir Israel, Marie Pacoud, Mickael Maucourt, Yassine El Fazaa, Daniel Jacob, Marc Lepetit and 3 more

Abstract read
In one paragraph

Article in Plant physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Marc BossenoInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.
Alexandre DembaInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.
Natasha Horta AraújoIRD, Plant Health Institute of Montpellier (PHIM), UMR IRD/SupAgro/INRAE/UM/CIRAD, Montpellier, France.ORCID 0000-0003-2400-6573
Dominique ColinetInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.ORCID 0000-0001-5122-5072
Abir IsraelInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.
Marie PacoudInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.
Mickael MaucourtBiologie du Fruit et Pathologie, Université de Bordeaux, INRAE, Villenave d'Ornon  France.ORCID 0000-0001-8260-880X
Yassine El FazaaInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.ORCID 0009-0003-2835-8063
Daniel JacobUR1268 BIA, BIBS Facility INRAE, Nantes, France.ORCID 0000-0002-6687-7169
Marc LepetitInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.ORCID 0000-0002-0372-5985
Dominique RolinBiologie du Fruit et Pathologie, Université de Bordeaux, INRAE, Villenave d'Ornon  France.
Renaud BrouquisseInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.ORCID 0000-0002-7818-9662
Alexandre BoscariInstitut Sophia Agrobiotech, UMR INRAE 1355, Université Côte d'Azur, CNRS, Sophia Antipolis  France.ORCID 0000-0002-9102-5443

Funding

Agence Nationale pour la Recherche ANR-07-BLAN-0117-02ANRCentre National de la Recherche Scientifique (CNRS)Institut National de la Recherche Agronomique (INRA)Université Côte d'Azur (UniCA)
6 · The paper itself

Abstract

Nitrate reductase (NR) is a key enzyme in nitrate assimilation, yet its function within nodules remains poorly understood. In Medicago truncatula, 3 NR genes, MtNR1, MtNR2, and MtNR3, exhibit distinct evolutionary origins and regulatory features. Phylogenetic analyses indicate that NR3-type genes, originated from a duplication of NR1 within the inverted repeat-lacking clade (IRLC) legumes, have lost the conserved phosphorylation sites critical for post-translational regulation. To assess the functional significance of these isoforms, we characterized single and double nr mutants obtained through Tnt1 transposon insertion under nitrate nutrition and during symbiosis. MtNR1 is the primary contributor to total NR activity, with nr1 and nr2 mutants retaining around 10% and 30% of wild-type levels, respectively. The nr1/nr2 double mutant shows an almost complete loss of NR activity and fails to survive under nitrate supply, demonstrating the essential and non-redundant roles of both isoforms. Under symbiotic conditions, single mutants displayed normal nodulation, whereas nodule development was nearly abolished in the double mutant despite continued MtNR3 expression. In addition to its role in nitrogen assimilation, single nr mutants showed increased sensitivity to hypoxic stress and impaired recovery of nitrogen fixation, revealing a role for NR in nodule energy metabolism through the phytoglobin-NO respiration pathway. We propose that the combined loss of NR1 and NR2 disrupts NO cycling linked to mitochondrial electron transport, thereby compromising the energy balance required for symbiosis under microoxic conditions. This work provides a framework to investigate NR diversification in legumes and opens perspectives for improving nitrogen fixation under environmental constraints.

Indexed as

Medicago truncatulaNitrate ReductaseSymbiosisGene Expression Regulation, PlantIsoenzymesMutationNitratesNitrogen FixationPhylogenyPlant ProteinsPlant Root NodulationRoot Nodules, PlantSinorhizobium melilotiIsoenzymesNitrate ReductaseNitratesPlant Proteins

Identifiers

PMID42302289
PMCPMC13332110

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.