ArticlePLoS pathogens2015
Molecular and functional analyses of a maize autoactive NB-LRR protein identify precise structural requirements for activity.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 145 citations in OpenAlex.
- The BTB/POZ-MATH Protein ZmBPM1 Interacts With Autophagy-related Protein ZmATG6 and Modulates the NLR Protein Rp1-D21-Mediated Defense Response in Maize.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Functional Dissection of a Wheat NLR Protein Reveals a Minimal Active Region and Key Regulatory Sites for Immune Signalling.Molecular plant pathology · 2026Article
- Dissection of Cell Death Induction byLife (Basel, Switzerland) · 2026Article
- The barley disease resistance proteinmicroPublication biology · 2026Article
- Decades' progress and prospects on maize functional genomics and molecular breeding.Science China. Life sciences · 2025Review
- Natural Variation of a Specific NLR Gene RGA4L Confers Strong Chilling Tolerance in Rice.Plant biotechnology journal · 2025Article
- A CNL protein forms an NLR pair with NRCX to modulate plant immunity.Stress biology · 2025Article
- Fine mapping and identification of causal alleles at the Ur-11 locus controlling rust resistance in common bean (Phaseolus vulgaris L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Assessment of Self-Activation and Inhibition of Wheat Coiled-Coil Domain Containing NLR Immune Receptor Yr10Plants (Basel, Switzerland) · 2025Article
- Insights ofFrontiers in plant science · 2025Article
- Identification and Functional Analysis of thePlants (Basel, Switzerland) · 2024Article
- Use of the Puccinia sorghi haustorial transcriptome to identify and characterize AvrRp1-D recognized by the maize Rp1-D resistance protein.PLoS pathogens · 2024Article
- Proteolysis in plant immunity.The Plant cell · 2024Review
- Implication of the LRR Domain in the Regulation and Activation of the NLRP3 Inflammasome.Cells · 2024Review
- Activation and Autoinhibition Mechanisms of NLR Immune Receptor Pi36 in Rice.International journal of molecular sciences · 2024Article
- A rapid and scalable approach to build synthetic repetitive hormone-responsive promoters.Plant biotechnology journal · 2024Article
- Pathogen perception and signaling in plant immunity.The Plant cell · 2024Review
- Two functional CC-NBS-LRR proteins from rye chromosome 6RS confer differential age-related powdery mildew resistance to wheat.Plant biotechnology journal · 2024Article
- Special issue: Genetics of maize-microbe interactions.Molecular plant pathology · 2023Article
- MG1 interacts with a protease inhibitor and confers resistance to rice root-knot nematode.Nature communications · 2023Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Plant disease resistance is often mediated by nucleotide binding-leucine rich repeat (NLR) proteins which remain auto-inhibited until recognition of specific pathogen-derived molecules causes their activation, triggering a rapid, localized cell death called a hypersensitive response (HR). Three domains are recognized in one of the major classes of NLR proteins: a coiled-coil (CC), a nucleotide binding (NB-ARC) and a leucine rich repeat (LRR) domains. The maize NLR gene Rp1-D21 derives from an intergenic recombination event between two NLR genes, Rp1-D and Rp1-dp2 and confers an autoactive HR. We report systematic structural and functional analyses of Rp1 proteins in maize and N. benthamiana to characterize the molecular mechanism of NLR activation/auto-inhibition. We derive a model comprising the following three main features: Rp1 proteins appear to self-associate to become competent for activity. The CC domain is signaling-competent and is sufficient to induce HR. This can be suppressed by the NB-ARC domain through direct interaction. In autoactive proteins, the interaction of the LRR domain with the NB-ARC domain causes de-repression and thus disrupts the inhibition of HR. Further, we identify specific amino acids and combinations thereof that are important for the auto-inhibition/activity of Rp1 proteins. We also provide evidence for the function of MHD2, a previously uncharacterized, though widely conserved NLR motif. This work reports several novel insights into the precise structural requirement for NLR function and informs efforts towards utilizing these proteins for engineering disease resistance.
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