Plant Toll/interleukin-1 receptor/resistance protein domains physically associate with enhanced disease susceptibility1 family proteins in immune signaling.

Plant Toll/interleukin-1 receptor/resistance protein (TIR) type nucleotide-binding and leucine-rich repeat immune receptors (NLRs) require enhanced disease susceptibility 1 (EDS1) family proteins and the helper NLRs NRG1 and ADR1 for immune activation. We show that the EDS1-SAG101b-NRG1 signaling pathway in is necessary for cell death signaling by TIR-NLRs from a range of plant species, suggesting a universal requirement for this module in TIR-NLR-mediated cell death in We also find that TIR domains physically associate with EDS1, PAD4, and SAG101 , independently of each other. Furthermore, NRG1 associates with SAG101b, but not with other EDS1 family members, via its C-terminal EP domain.

Subcellular localization requirements and specificities for plant immune receptor Toll-interleukin-1 receptor signaling.

Recent work shed light on how plant intracellular immune receptors of the nucleotide-binding leucine-rich repeat (NLR) family are activated upon pathogen effector recognition to trigger immune responses. Activation of Toll-interleukin-1 receptor (TIR) domain-containing NLRs (TNLs) induces receptor oligomerization and close proximity of the TIR domain, which is required for TIR enzymatic activity. TIR-catalyzed small signaling molecules bind to EDS1 family heterodimers and subsequently activate downstream helper NLRs, which function as Ca permeable channel to activate immune responses eventually leading to cell death.

Invited review: Current enteric methane mitigation options.

Ruminant livestock are an important source of anthropogenic methane (CH). Decreasing the emissions of enteric CH from ruminant production is strategic to limit the global temperature increase to 1.5°C by 2050.

Connecting the dots between cell surface- and intracellular-triggered immune pathways in plants.

Plants can detect microbial molecules via surface-localized pattern-recognition receptors (PRRs) and intracellular immune receptors from the nucleotide-binding, leucine-rich repeat receptor (NLR) family. The corresponding pattern-triggered (PTI) and effector-triggered (ETI) immunity were long considered separate pathways, although they converge on largely similar cellular responses, such as calcium influx and overlapping gene reprogramming. A number of studies recently uncovered genetic and molecular interconnections between PTI and ETI, highlighting the complexity of the plant immune network.

Correction: Autoacetylation of the Ralstonia solanacearum Effector PopP2 Targets a Lysine Residue Essential for RRS1-R-Mediated Immunity in Arabidopsis.

[This corrects the article DOI: 10.1371/journal.ppat.

Improved accuracy and reduced uncertainty in greenhouse gas inventories by refining the IPCC emission factor for direct N O emissions from nitrogen inputs to managed soils.

Most national GHG inventories estimating direct N O emissions from managed soils rely on a default Tier 1 emission factor (EF ) amounting to 1% of nitrogen inputs. Recent research has, however, demonstrated the potential for refining the EF considering variables that are readily available at national scales. Building on existing reviews, we produced a large dataset (n = 848) enriched in dry and low latitude tropical climate observations as compared to former global efforts and disaggregated the EF according to most meaningful controlling factors.

Can N O emissions offset the benefits from soil organic carbon storage?

To respect the Paris agreement targeting a limitation of global warming below 2°C by 2100, and possibly below 1.5°C, drastic reductions of greenhouse gas emissions are mandatory but not sufficient. Large-scale deployment of other climate mitigation strategies is also necessary.

Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants.

Plant and animal intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors detect pathogen-derived molecules and activate defense. Plant NLRs can be divided into several classes based upon their N-terminal signaling domains, including TIR (Toll-like, Interleukin-1 receptor, Resistance protein)- and CC (coiled-coil)-NLRs. Upon ligand detection, mammalian NAIP and NLRC4 NLRs oligomerize, forming an inflammasome that induces proximity of its N-terminal signaling domains.

Climate and Soil Characteristics Determine Where No-Till Management Can Store Carbon in Soils and Mitigate Greenhouse Gas Emissions.

Adoption of no-till management on croplands has become a controversial approach for storing carbon in soil due to conflicting findings. Yet, no-till is still promoted as a management practice to stabilize the global climate system from additional change due to anthropogenic greenhouse gas emissions, including the 4 per mille initiative promoted through the UN Framework Convention on Climate Change. We evaluated the body of literature surrounding this practice, and found that SOC storage can be higher under no-till management in some soil types and climatic conditions even with redistribution of SOC, and contribute to reducing net greenhouse gas emissions.

Loss of by somatic exchange in stem rust leads to virulence for resistance in wheat.

Race-specific resistance genes protect the global wheat crop from stem rust disease caused by f. sp. () but are often overcome owing to evolution of new virulent races of the pathogen.

Characterization of NO emissions and associated microbial communities from the ant mounds in soils of a humid tropical rainforest.

Tropical rainforest soils harbor a considerable diversity of soil fauna that contributes to emissions of NO. Despite their ecological dominance, there is limited information available about the contribution of epigeal ant mounds to NO emissions in these tropical soils. This study aimed to determine whether ant mounds contribute to local soil N emissions in the tropical humid rainforest.

Crystal structure of the Melampsora lini effector AvrP reveals insights into a possible nuclear function and recognition by the flax disease resistance protein P.

The effector protein AvrP is secreted by the flax rust fungal pathogen (Melampsora lini) and recognized specifically by the flax (Linum usitatissimum) P disease resistance protein, leading to effector-triggered immunity. To investigate the biological function of this effector and the mechanisms of specific recognition by the P resistance protein, we determined the crystal structure of AvrP. The structure reveals an elongated zinc-finger-like structure with a novel interleaved zinc-binding topology.

What Do We Know About NOD-Like Receptors in Plant Immunity?

The first plant disease resistance (R) genes were identified and cloned more than two decades ago. Since then, many more R genes have been identified and characterized in numerous plant pathosystems. Most of these encode members of the large family of intracellular NLRs (NOD-like receptors), which also includes animal immune receptors.

Multiple functional self-association interfaces in plant TIR domains.

The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 from Here we show that the crystal structure of the TIR domain from the NLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices αD and αE (DE interface) and an RPS4-like interface involving helices αA and αE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4.

Cytosolic activation of cell death and stem rust resistance by cereal MLA-family CC-NLR proteins.

Plants possess intracellular immune receptors designated "nucleotide-binding domain and leucine-rich repeat" (NLR) proteins that translate pathogen-specific recognition into disease-resistance signaling. The wheat immune receptors Sr33 and Sr50 belong to the class of coiled-coil (CC) NLRs. They confer resistance against a broad spectrum of field isolates of Puccinia graminis f.

Comparative Analysis of the Flax Immune Receptors L6 and L7 Suggests an Equilibrium-Based Switch Activation Model.

NOD-like receptors (NLRs) are central components of the plant immune system. L6 is a Toll/interleukin-1 receptor (TIR) domain-containing NLR from flax (Linum usitatissimum) conferring immunity to the flax rust fungus. Comparison of L6 to the weaker allele L7 identified two polymorphic regions in the TIR and the nucleotide binding (NB) domains that regulate both effector ligand-dependent and -independent cell death signaling as well as nucleotide binding to the receptor.

From forest to cropland and pasture systems: a critical review of soil organic carbon stocks changes in Amazonia.

The impact of deforestation on soil organic carbon (SOC) stocks is important in the context of climate change and agricultural soil use. Trends of SOC stock changes after agroecosystem establishment vary according to the spatial scale considered, and factors explaining these trends may differ sometimes according to meta-analyses. We have reviewed the knowledge about changes in SOC stocks in Amazonia after the establishment of pasture or cropland, sought relationships between observed changes and soil, climatic variables and management practices, and synthesized the δ C measured in pastures.

A novel conserved mechanism for plant NLR protein pairs: the "integrated decoy" hypothesis.

Plant immunity is often triggered by the specific recognition of pathogen effectors by intracellular nucleotide-binding, leucine-rich repeat receptors (NLR). Plant NLRs contain an N-terminal signaling domain that is mostly represented by either a Toll-interleukin1 receptor (TIR) domain or a coiled coil (CC) domain. In many cases, single NLR proteins are sufficient for both effector recognition and signaling activation.

The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance.

Plant resistance proteins of the class of nucleotide-binding and leucine-rich repeat domain proteins (NB-LRRs) are immune sensors which recognize pathogen-derived molecules termed avirulence (AVR) proteins. We show that RGA4 and RGA5, two NB-LRRs from rice, interact functionally and physically to mediate resistance to the fungal pathogen Magnaporthe oryzae and accomplish different functions in AVR recognition. RGA4 triggers an AVR-independent cell death that is repressed in the presence of RGA5 in both rice protoplasts and Nicotiana benthamiana.

Structural basis for assembly and function of a heterodimeric plant immune receptor.

Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate.

Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana.

The Toll/interleukin-1 receptor (TIR) domain is a protein-protein interaction domain that is found in both animal and plant immune receptors. The N-terminal TIR domain from the nucleotide-binding (NB)-leucine-rich repeat (LRR) class of plant disease-resistance (R) proteins has been shown to play an important role in defence signalling. Recently, the crystal structure of the TIR domain from flax R protein L6 was determined and this structure, combined with functional studies, demonstrated that TIR-domain homodimerization is a requirement for function of the R protein L6.

Brazilian beef cattle feedlot manure management: a country survey.

No information regarding the management of manure from beef cattle feedlots is available for Brazil. To fill this knowledge gap, a survey of 73 feedlots was conducted in 7 Brazilian states. In this survey, questions were asked regarding animal characteristics, their diets, and manure handling management from generation to disposal.

Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.

L locus resistance (R) proteins are nucleotide binding (NB-ARC) leucine-rich repeat (LRR) proteins from flax (Linum usitatissimum) that provide race-specific resistance to the causal agent of flax rust disease, Melampsora lini. L5 and L6 are two alleles of the L locus that directly recognize variants of the fungal effector AvrL567. In this study, we have investigated the molecular details of this recognition by site-directed mutagenesis of AvrL567 and construction of chimeric L proteins.

N-terminal motifs in some plant disease resistance proteins function in membrane attachment and contribute to disease resistance.

To investigate the role of N-terminal domains of plant disease resistance proteins in membrane targeting, the N termini of a number of Arabidopsis and flax disease resistance proteins were fused to green fluorescent protein (GFP) and the fusion proteins localized in planta using confocal microscopy. The N termini of the Arabidopsis RPP1-WsB and RPS5 resistance proteins and the PBS1 protein, which is required for RPS5 resistance, targeted GFP to the plasma membrane, and mutation of predicted myristoylation and potential palmitoylation sites resulted in a shift to nucleocytosolic localization. The N-terminal domain of the membrane-attached Arabidopsis RPS2 resistance protein was targeted incompletely to the plasma membrane.