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1.
PLoS Pathog ; 13(4): e1006284, 2017 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-28406987

RESUMEN

Plant-parasitic nematodes are destructive pests causing losses of billions of dollars annually. An effective plant defence against pathogens relies on the recognition of pathogen-associated molecular patterns (PAMPs) by surface-localised receptors leading to the activation of PAMP-triggered immunity (PTI). Extensive studies have been conducted to characterise the role of PTI in various models of plant-pathogen interactions. However, far less is known about the role of PTI in roots in general and in plant-nematode interactions in particular. Here we show that nematode-derived proteinaceous elicitor/s is/are capable of inducing PTI in Arabidopsis in a manner dependent on the common immune co-receptor BAK1. Consistent with the role played by BAK1, we identified a leucine-rich repeat receptor-like kinase, termed NILR1 that is specifically regulated upon infection by nematodes. We show that NILR1 is essential for PTI responses initiated by nematodes and nilr1 loss-of-function mutants are hypersusceptible to a broad category of nematodes. To our knowledge, NILR1 is the first example of an immune receptor that is involved in induction of basal immunity (PTI) in plants or in animals in response to nematodes. Manipulation of NILR1 will provide new options for nematode control in crop plants in future.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/enzimología , Interacciones Huésped-Parásitos , Enfermedades de las Plantas/inmunología , Inmunidad de la Planta , Proteínas Serina-Treonina Quinasas/metabolismo , Tylenchoidea/fisiología , Animales , Arabidopsis/citología , Arabidopsis/genética , Arabidopsis/inmunología , Proteínas de Arabidopsis/genética , Raíces de Plantas/citología , Raíces de Plantas/enzimología , Raíces de Plantas/genética , Raíces de Plantas/inmunología , Proteínas Quinasas/genética , Proteínas Quinasas/metabolismo , Proteínas Serina-Treonina Quinasas/genética , Transducción de Señal
2.
Plant J ; 77(5): 688-99, 2014 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-24372773

RESUMEN

Polyadenylation of pre-mRNAs by poly(A) polymerase (PAPS) is a critical process in eukaryotic gene expression. As found in vertebrates, plant genomes encode several isoforms of canonical nuclear PAPS enzymes. In Arabidopsis thaliana these isoforms are functionally specialized, with PAPS1 affecting both organ growth and immune response, at least in part by the preferential polyadenylation of subsets of pre-mRNAs. Here, we demonstrate that the opposite effects of PAPS1 on leaf and flower growth reflect the different identities of these organs, and identify a role for PAPS1 in the elusive connection between organ identity and growth patterns. The overgrowth of paps1 mutant petals is due to increased recruitment of founder cells into early organ primordia, and suggests that PAPS1 activity plays unique roles in influencing organ growth. By contrast, the leaf phenotype of paps1 mutants is dominated by a constitutive immune response that leads to increased resistance to the biotrophic oomycete Hyaloperonospora arabidopsidis and reflects activation of the salicylic acid-independent signalling pathway downstream of ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1)/PHYTOALEXIN DEFICIENT4 (PAD4). These findings provide an insight into the developmental and physiological basis of the functional specialization amongst plant PAPS isoforms.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/fisiología , Flores/crecimiento & desarrollo , Hojas de la Planta/inmunología , Polinucleotido Adenililtransferasa/metabolismo , Proteínas de Arabidopsis/genética , Hidrolasas de Éster Carboxílico/metabolismo , Proteínas de Unión al ADN/metabolismo , Mutación , Inmunidad de la Planta , Poliadenilación , Polinucleotido Adenililtransferasa/genética , Ácido Salicílico/metabolismo
3.
Plant Cell ; 23(6): 2440-55, 2011 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-21693696

RESUMEN

Recognition of pathogen-associated molecular patterns (PAMPs) by surface-localized pattern recognition receptors (PRRs) constitutes an important layer of innate immunity in plants. The leucine-rich repeat (LRR) receptor kinases EF-TU RECEPTOR (EFR) and FLAGELLIN SENSING2 (FLS2) are the PRRs for the peptide PAMPs elf18 and flg22, which are derived from bacterial EF-Tu and flagellin, respectively. Using coimmunoprecipitation and mass spectrometry analyses, we demonstrated that EFR and FLS2 undergo ligand-induced heteromerization in planta with several LRR receptor-like kinases that belong to the SOMATIC-EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) family, including BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE1/SERK3 (BAK1/SERK3) and BAK1-LIKE1/SERK4 (BKK1/SERK4). Using a novel bak1 allele that does not exhibit pleiotropic defects in brassinosteroid and cell death responses, we determined that BAK1 and BKK1 cooperate genetically to achieve full signaling capability in response to elf18 and flg22 and to the damage-associated molecular pattern AtPep1. Furthermore, we demonstrated that BAK1 and BKK1 contribute to disease resistance against the hemibiotrophic bacterium Pseudomonas syringae and the obligate biotrophic oomycete Hyaloperonospora arabidopsidis. Our work reveals that the establishment of PAMP-triggered immunity (PTI) relies on the rapid ligand-induced recruitment of multiple SERKs within PRR complexes and provides insight into the early PTI signaling events underlying this important layer of plant innate immunity.


Asunto(s)
Proteínas de Arabidopsis/inmunología , Arabidopsis/enzimología , Arabidopsis/inmunología , Inmunidad Innata , Oomicetos/patogenicidad , Enfermedades de las Plantas/inmunología , Proteínas Quinasas/metabolismo , Proteínas Serina-Treonina Quinasas/inmunología , Secuencia de Aminoácidos , Arabidopsis/genética , Arabidopsis/microbiología , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Ligandos , Datos de Secuencia Molecular , Complejos Multienzimáticos/genética , Complejos Multienzimáticos/metabolismo , Oomicetos/inmunología , Péptidos/genética , Péptidos/metabolismo , Proteínas Quinasas/genética , Proteínas Serina-Treonina Quinasas/genética , Pseudomonas syringae/inmunología , Pseudomonas syringae/patogenicidad , Proteínas Recombinantes de Fusión/metabolismo , Transducción de Señal
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