RESUMEN
Endogenous signalling peptides play diverse roles during plant growth, development and stress responses. Research in recent years has unravelled peptides with previously known growth-regulatory function as immune-modulatory agents that fine-tune pattern-triggered immunity (PTI). Moreover, peptides that are long known as endogenous danger signals were recently implicated in growth and development. In analogy to metazoan systems these peptides are referred to as phytocytokines. In this review we will highlight recent progress made on our understanding of phytocytokines simultaneously regulating growth and PTI which shows the complex interplay of peptide signalling pathways regulating multiple aspects of a plant's life.
Asunto(s)
Enfermedades de las Plantas , Inmunidad de la Planta , Animales , Péptidos , Desarrollo de la Planta , Inmunidad de la Planta/fisiología , Transducción de Señal/fisiologíaRESUMEN
Plants utilise intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors to detect pathogen effectors and activate local and systemic defence. NRG1 and ADR1 "helper" NLRs (RNLs) cooperate with enhanced disease susceptibility 1 (EDS1), senescence-associated gene 101 (SAG101) and phytoalexin-deficient 4 (PAD4) lipase-like proteins to mediate signalling from TIR domain NLR receptors (TNLs). The mechanism of RNL/EDS1 family protein cooperation is not understood. Here, we present genetic and molecular evidence for exclusive EDS1/SAG101/NRG1 and EDS1/PAD4/ADR1 co-functions in TNL immunity. Using immunoprecipitation and mass spectrometry, we show effector recognition-dependent interaction of NRG1 with EDS1 and SAG101, but not PAD4. An EDS1-SAG101 complex interacts with NRG1, and EDS1-PAD4 with ADR1, in an immune-activated state. NRG1 requires an intact nucleotide-binding P-loop motif, and EDS1 a functional EP domain and its partner SAG101, for induced association and immunity. Thus, two distinct modules (NRG1/EDS1/SAG101 and ADR1/EDS1/PAD4) mediate TNL receptor defence signalling.
Asunto(s)
Proteínas de Arabidopsis/metabolismo , Hidrolasas de Éster Carboxílico/metabolismo , Proteínas de Unión al ADN/metabolismo , Neurregulina-1/metabolismo , Inmunidad de la Planta/fisiología , Receptores Inmunológicos/metabolismo , Arabidopsis/genética , Arabidopsis/metabolismo , Arabidopsis/microbiología , Proteínas de Arabidopsis/química , Proteínas de Arabidopsis/genética , Hidrolasas de Éster Carboxílico/química , Hidrolasas de Éster Carboxílico/genética , Muerte Celular , Proteínas de Unión al ADN/química , Proteínas de Unión al ADN/genética , Inmunidad Innata , Neurregulina-1/química , Neurregulina-1/genética , Enfermedades de las Plantas/inmunología , Enfermedades de las Plantas/microbiología , Inmunidad de la Planta/genética , Plantas Modificadas Genéticamente , Dominios Proteicos , Pseudomonas syringae , Receptores Inmunológicos/química , Receptores Inmunológicos/genética , Transducción de Señal , Nicotiana/genética , Nicotiana/metabolismoRESUMEN
Plant nucleotide binding/leucine-rich repeat (NLR) immune receptors are activated by pathogen effectors to trigger host defenses and cell death. Toll-interleukin 1 receptor domain NLRs (TNLs) converge on the ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1) family of lipase-like proteins for all resistance outputs. In Arabidopsis (Arabidopsis thaliana) TNL-mediated immunity, AtEDS1 heterodimers with PHYTOALEXIN DEFICIENT4 (AtPAD4) transcriptionally induced basal defenses. AtEDS1 uses the same surface to interact with PAD4-related SENESCENCE-ASSOCIATED GENE101 (AtSAG101), but the role of AtEDS1-AtSAG101 heterodimers remains unclear. We show that AtEDS1-AtSAG101 functions together with N REQUIRED GENE1 (AtNRG1) coiled-coil domain helper NLRs as a coevolved TNL cell death-signaling module. AtEDS1-AtSAG101-AtNRG1 cell death activity is transferable to the Solanaceous species Nicotiana benthamiana and cannot be substituted by AtEDS1-AtPAD4 with AtNRG1 or AtEDS1-AtSAG101 with endogenous NbNRG1. Analysis of EDS1-family evolutionary rate variation and heterodimer structure-guided phenotyping of AtEDS1 variants and AtPAD4-AtSAG101 chimeras identify closely aligned É-helical coil surfaces in the AtEDS1-AtSAG101 partner C-terminal domains that are necessary for reconstituted TNL cell death signaling. Our data suggest that TNL-triggered cell death and pathogen growth restriction are determined by distinctive features of EDS1-SAG101 and EDS1-PAD4 complexes and that these signaling machineries coevolved with other components within plant species or clades to regulate downstream pathways in TNL immunity.