ArticleThe Journal of biological chemistry2015
The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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.
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.
Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- A CC-NB-ARC-LRR Gene Regulates Bract Morphology in Cotton.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Spotlight on Plant Bromodomain Proteins.Biology · 2023Review
- Review
- GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif.Plant physiology · 2022Article
- Extreme Resistance to Viruses in Potato and Soybean.Frontiers in plant science · 2021Review
- Single-stranded oligodeoxynucleotides induce plant defence in Arabidopsis thaliana.Annals of botany · 2020Article
- A DNA-Binding Bromodomain-Containing Protein Interacts with and Reduces Rx1-Mediated Immune Response to Potato Virus X.Plant communications · 2020Article
- A bacteriophage mimic of the bacterial nucleoid-associated protein Fis.The Biochemical journal · 2020Article
- Perspectives on intracellular perception of plant viruses.Molecular plant pathology · 2019Review
- GalaxyRefine2: simultaneous refinement of inaccurate local regions and overall protein structure.Nucleic acids research · 2019Article
- Activation of immune receptor Rx1 triggers distinct immune responses culminating in cell death after 4 hours.Molecular plant pathology · 2019Article
- An EDS1 heterodimer signalling surface enforces timely reprogramming of immunity genes in Arabidopsis.Nature communications · 2019Article
- Distinct Roles of Non-Overlapping Surface Regions of the Coiled-Coil Domain in the Potato Immune Receptor Rx1.Plant physiology · 2018Article
- Genomic and epigenomic immunity in common bean: the unusual features of NB-LRR gene family.DNA research : an international journal for rapid publication of reports on genes and genomes · 2018Article
- Extreme resistance: The GLK-Rx1 alliance.The Journal of biological chemistry · 2018Article
- The intracellular immune receptor Rx1 regulates the DNA-binding activity of a Golden2-like transcription factor.The Journal of biological chemistry · 2018Article
- Mapping of a Major QTL forFrontiers in plant science · 2018Article
- The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice.The Plant cell · 2017Article
- Animal NLRs provide structural insights into plant NLR function.Annals of botany · 2017Review
- Cell death triggering and effector recognition by Sw-5 SD-CNL proteins from resistant and susceptible tomato isolines to Tomato spotted wilt virus.Molecular plant pathology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
Plant nucleotide-binding leucine-rich repeat (NLR) proteins enable cells to respond to pathogen attack. Several NLRs act in the nucleus; however, conserved nuclear targets that support their role in immunity are unknown. Previously, we noted a structural homology between the nucleotide-binding domain of NLRs and DNA replication origin-binding Cdc6/Orc1 proteins. Here we show that the NB-ARC (nucleotide-binding, Apaf-1, R-proteins, and CED-4) domain of the Rx1 NLR of potato binds nucleic acids. Rx1 induces ATP-dependent bending and melting of DNA in vitro, dependent upon a functional P-loop. In situ full-length Rx1 binds nuclear DNA following activation by its cognate pathogen-derived effector protein, the coat protein of potato virus X. In line with its obligatory nucleocytoplasmic distribution, DNA binding was only observed when Rx1 was allowed to freely translocate between both compartments and was activated in the cytoplasm. Immune activation induced by an unrelated NLR-effector pair did not trigger an Rx1-DNA interaction. DNA binding is therefore not merely a consequence of immune activation. These data establish a role for DNA distortion in Rx1 immune signaling and define DNA as a molecular target of an activated NLR.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.