Evidence map›Paper›PMID 40988468›Full record

ArticlePlant, cell & environment2026

The Arabidopsis deNADding Enzyme DXO1 Modulates the Plant Immunity Response.

Anna Golisz-Mocydlarz, Monika Zakrzewska-Placzek, Michal Krzyszton, Nataliia Diachenko, Justyna Piotrowska, Wiktoria Kalbarczyk, Agnieszka Marasek-Ciolakowska, Joanna Kufel

Abstract read
In one paragraph

Article in Plant, cell & environment, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Arabidopsis DXO1- and RNMT1-Mediated mPlant, cell & environment · 2026
    Article
  2. Article
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

8 authors.

Anna Golisz-MocydlarzUniversity of Warsaw, Faculty of Biology, Institute of Genetics and Biotechnology, Warsaw, Poland.ORCID https://orcid.org/0000-0002-7539-1830
Monika Zakrzewska-PlaczekUniversity of Warsaw, Faculty of Biology, Institute of Genetics and Biotechnology, Warsaw, Poland.ORCID https://orcid.org/0000-0002-0538-7721
Michal KrzysztonPolish Academy of Sciences, Institute of Biochemistry and Biophysics, Laboratory of Seeds Molecular Biology, Warsaw, Poland.ORCID https://orcid.org/0000-0002-9795-5588
Nataliia DiachenkoUniversity of Warsaw, Faculty of Biology, Institute of Genetics and Biotechnology, Warsaw, Poland.
Justyna PiotrowskaPolish Academy of Sciences, Institute of Biochemistry and Biophysics, Laboratory of Plant Protein Homeostasis, Warsaw, Poland.ORCID https://orcid.org/0000-0001-6135-5110
Wiktoria KalbarczykUniversity of Warsaw, Faculty of Biology, Institute of Genetics and Biotechnology, Warsaw, Poland.
Agnieszka Marasek-CiolakowskaThe National Institute of Horticultural Research, Skierniewice, Poland.ORCID https://orcid.org/0000-0001-9349-2566
Joanna KufelUniversity of Warsaw, Faculty of Biology, Institute of Genetics and Biotechnology, Warsaw, Poland.ORCID https://orcid.org/0000-0001-6810-2749

Funding

This study was supported through grants from National Science Centre UMO-2014/13/B/NZ3/00405 to A.G.-M., UMO-2018/29/B/NZ3/01980 and UMO-2021/40/Q/NZ1/00014 to J.K.
6 · The paper itself

Abstract

DXO1, the only DXO homolog in Arabidopsis, due to its plant-specific features, exhibits strong deNADding enzymatic activity but has no apparent role in 5' QC. Despite its important contribution to plant RNA metabolism, the direct impact of DXO1 enzymatic activity on cellular processes appears surprisingly limited. Notably, most molecular and morphological changes observed so far in dxo1 mutant plants depended on the plant-specific N-terminal domain of the protein. Our investigation into the role of DXO1 in response to biotic stress, specifically its susceptibility to Pseudomonas syringae pv. tomato DC3000 infection, unexpectedly revealed the importance of DXO1 enzymatic activity in the plant immune response. We observed that dxo1-2 knockout mutant and transgenic dxo1-2 lines expressing a DXO1 variant either catalytically inactive or lacking the N-terminal domain exhibited enhanced resistance to Pst, accompanied by marked changes in the expression of key pathogenesis markers. Also, other markers of plant immunity, such as callose deposition and production of reactive oxygen species, were strongly induced by PAMPs elf18 and flg22. These results strongly suggest that both DXO1 features, the N-terminal domain and its catalytic site, contribute to the regulation of plant immunity. This is the first observation revealing the involvement of DXO1 enzymatic activity in plant physiology. Moreover, our analyses showed that dxo1-2 mutation altered the expression of a large group of defense-related genes, affected the stability of mRNAs, and delayed the activation of MAP kinases. Therefore, we postulate that DXO1 protein deregulates defense against Pst infection at both the transcriptional and posttranscriptional levels.

Indexed as

ArabidopsisArabidopsis ProteinsExoribonucleasesPlant DiseasesPlant ImmunityChloroplast ProteinsMutationPathogen-Associated Molecular Pattern MoleculesPlants, Genetically ModifiedPseudomonas syringaeReactive Oxygen SpeciesArabidopsis ProteinsAT4G17620 protein, ArabidopsisChloroplast ProteinsExoribonucleasesPathogen-Associated Molecular Pattern MoleculesReactive Oxygen SpeciesArabidopsis thalianabiotic stressDXO1plant immunityPseudomonas syringae

Identifiers

PMID40988468
PMCPMC12675986

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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.